Macromolecular crystallography in India. A historical overview

Journal of the Indian Institute of Science

Volumn 87, Issue 2, 2007, Pages 261-277

  Vijayan, M ^a  

^a INDIAN INSTITUTE OF SCIENCE   (India)

Author keywords

[No Author keywords available]

Indexed keywords

MACROMOLECULAR CRYSTALLOGRAPHY; MICROBIAL PATHOGENS; STRUCTURAL BIOLOGY;

CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; MOLECULAR INTERACTIONS; PROBLEM SOLVING; SPECTRUM ANALYSIS;

MACROMOLECULES;

EID: 38549105974     PISSN: 09704140     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review

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109. Sankaranarayanan, R., Biswal, B. K. and Vijayan, M. A new relaxed state in horse methemoglobin characterized by crystallographic studies. Proteins: Struct. Funct. Bioinf. 60, 547-551 (2005).
110. Ravichandran, S., Dasgupta, J., Chakrabarti, C., Ghosh, S., Singh, M. and Dattagupta, J. K. The role of Asn 14 in the stability and conformation of the reactive-site loop of winged bean chymotrypsin inhibitor: crystal structures of two point mutants Asn14-→ Lys and Asn14-→ Asp. Protein Eng. 14, 349-357 (2001).
111. Biswas, S., Chakrabarti, C., Kundu, S., Jagannadham, M. V. and Dattagupta, J. K. Proposed Amino Acid Sequence and the 1.63 Å X-ray Crystal structure of a plant cysteine protease, ervatamin B: some insights into the structural basis of its stability and substrate specificity. Proteins: Struct. Funct. Genet. 51, 489-497 (2003).
112. Guha Thakurta, P., Choudhury, D., Dasgupta, R. and Dattagupta, J. K. (2004). Structural basis of the unusual stability and substrate specificity of ervatamin C, a plant cysteine protease from Ervatamia coronaria. Biochemistry 43, 1532-1540 (2004).
113. Khamrui, S., Dasgupta, J., Dattagupta, J. K. and Sen, U. Single mutation at Pl of a chymotrypsin inhibitor changes it to a trypsin inhibitor: X-ray structural (2.15 Å) and biochemical basis. Biochim. Biophys. Acta 1752, 65-72 (2005).
114. Dasgupta, J., Khamrui, S., Dattagupta, J. K. and Sen, U. Spacer Asn determines the fate of Kunitz (STI) inhibitors, as revealed by structural and biochemical studies on WCI mutants. Biochemistry 45, 6783-6792 (2006).
115. Prasad, B. V. L. S. and Suguna, K. Role of water molecules in the structure and function of aspartic proteinases. Acta Cryst. D58, 250-258 (2002).
116. Prasad, B. V. L. S. and Suguna, K. Effect of pH on the structure of rhizopuspepsin. Acta Cryst. D59, 1755-1761 (2003).
117. Syed Ibrahim, B. and Vasantha Pattabhi. Crystal structure of trypsin-turkey egg white inhibitor complex. Biochem. Biophys. Res. Commun. 313, 8-16 (2003).
118. Shamaladevi, N. and Vasantha Pattabhi. Secondary binding site of trypsin: revealed by crystal structure of trypsin-peptide complex. J. Biomol Struct. Dyn. 22, 635-642 (2005).
119. Syed Ibrahim, B. and Vasantha Pattabhi. Trypsin inhibition by a peptide hormone: crystal structure of trypsin-vasopressin complex. J. Mol. Biol. 348, 1191-1198 (2005).
120. 2 from Daboia russelli pulchella at 2.4 Å resolution. J. Mol. Biol. 296, 1117-1126 (2000).
121. Singh, G., Gourinath, S., Sharma, S., Paramasivam, M., Srinivasan, A. and Singh, T. P. Structure of a basic phospholipase A2 from Bangarus Caeruleus (common krait: KPLA2) at 2.4Å resolution: identification and characterization of its pharmacological sites. J. Mol. Biol. 307, 1049-1059 (2001).
122. Bhanumathi, S., Rajashankar, K. R., Noetzel, C., Aleksiev, B., Singh, T. P., Genov, N. and Betzel, Ch. Crystal structure of the neurotoxic complex vipoxin at 1.4 Å resolution. Acta Cryst D57, 1552-1559 (2001).
123. 2 from Daboia russelli pulchella at 1.9 Å resolution. Acta Cryst. D57, 1793-1798 (2001).
124. 2 in a complex with vitamin E at 1.7 A resolution. J. Mol. Biol. 320, 215-222 (2002).
125. 2 and aristolochic acid at 1.7 Å resolution. Biochemistry 41, 10914-10919 (2002).
126. 2 and a designed peptide Leu-Ala-Ile-Tyr-Ser (LAIYS). Acta Cryst D58, 1813-1819 (2002).
127. 2 and designed peptide Phe-Leu-SerTyr-Lys at 1.8Å resolution. J. Biol. Chem. 277, 18641-18647 (2002).
128. Perbandt, M., Tsai, I-H., Fuchs, A., Bhanumathi, S., Rajashankar, K. R., Georgieva, D., Kalkura, N., Singh, T. P., Genov, N. and Betzel, Ch. Crystal structure of the heterodimeric neurotoxic complex viperatoxin F (RV-4/RV-7) from the venom of Vipera russelli formosensis at 1.9 Å resolution. Acta Cryst. D59, 1679-1687 (2003).
129. 2 from Naja naja sagittifera and a designed peptide inhibitor at 1.9 Å resolution. Biochemistry 42, 11701-11706 (2003).
130. Bilgrami, S., Tomar, S., Yadav, S., Kaur, P., Kumar, J., Jabeen, T., Sharma, S. and Singh, T. P. Crystal structure of schistatin, a disintegrin homodimer from saw-scaled viper (Echis carinatus) at 2.5 Å resolution. J. Mol. Biol. 341, 829-837 (2004).
131. 2 and an anti-inflammatory agent oxyphenbutazone at 1.6 A resolution. Biochemistry 43, 14577-14583 (2004).
132. Jasti, J., Paramasivam, M., Srinivasan, A. and Singh, T. P. Structure of an acidic phospholipase A2 from Indian sawscaled viper (Echis carinatus) at 2.6 Å resolution reveals a novel intermolecular interaction. Acta Cryst. D60, 66-72 (2004).
133. Jasti, J., Paramasivam, M., Srinivasan, A. and Singh, T. P. Crystal structure of echicetin from Echis carinatus (Indian saw-scaled viper) at 2.4 A resolution. J. Mol. Biol. 335, 167-176 (2004).
134. 2 from Bangarus caeruleus at 2.1 Å resolution. J. Struc. Biol. 149, 264-276 (2005).
135. 2 from common krait (Bangarus caeruleus) at 2.5 Å resolution. Acta Cryst. F61, 8-13 (2005).
136. Singh, G., Jasti, J., Sarvanan, K., Sharma, S., Kaur, P., Srinivasan, A. and Singh, T. P. Crystal structure of the complex formed between a group I phospholipase A2 and a naturally occurring fatty acid at 2.7 Å resolution. Protein Sci. 14, 395-400 (2005).
137. Jabeen, T., Sharma, S., Singh, N., Singh, R.K., Verma, A.K., Paramasivam, M., Srinivasan, A. and Singh, T. P. Structure of the zinc-induced heterodimer of two calcium-free isoforms of phospholipase A2 from Naja naja sagittifera at 2.7 Å resolution. Acta Cryst. D61, 302-308 (2005).
138. Jabeen, T., Sharma, S., Singh, N., Singh, R. K., Verma, A. K., Paramasivam, M., Srinivasan, A. and Singh, T. P. Crystal structure of a calcium-induced dimer of two isoforms of cobra phospholipase A2 at 1.6Å resolution. Proteins: Struct. Funct. Bioinf. 59, 856-863 (2005).
139. Jabeen, T., Singh, N., Singh, R. K., Jasti, J., Sharma, S., Kaur, P., Srinivasan, A. and Singh, T. P. Crystal structure of a heterodimer of phospholipase A2 from Naja naja sagittifera at 2.3 A resolution reveals the presence of a new PLA2-like protein with a novel Cys32-Cys49 disulfide bridge. Proteins: Struct. Funct. Bioinf. 59, 2689-2698 (2005).
140. Bilgrami, S., Kaur, P., Yadav, S., Sharma, S., Perbandt, M., Betzel Ch. and Singh, T. P. Crystal structure of the disintegrin heterodimer from saw-scaled viper (Echis carinatus) at 1.9 Å resolution. Biochemistry 44, 11058-11066 (2005).
141. Karthikeyan, S., Yadav, S., Paramasivam, M., Srinivasan, A. and Singh, T. P. Structure of buffalo lactoferrin at 3.3 Å resolution at 277 K. Acta Cryst. D56, 684-694 (2000).
142. Sharma, A. K., Kumar, S., Sharma, V., Nagpal, A., Singh, N., Tamboli, I., Mani, I., Raman, G. and Singh, T. P. Lactoferrinmelanin interaction and its possible implications in melanin polymerization: Crystal structure of the complex formed between mare lactoferrin and melanin monomers at 2.7 Å resolution. Proteins: Struct. Funct. Genet. 45, 229-236 (2001).
143. Khan, J. A., Kumar, P., Paramsivam, M., Yadav, R. S., Sahni, M. S., Sharma, S., Srinivasan, A. and Singh, T. P. Camel lactoferrin-A transferrin-cum-lactoferrin: crystal structure of camel apolactoferrin at 2.6 Å resolution and structural basis of its dual role. J. Mol. Biol 309, 751-782 (2001).
144. 3+ binding pathway of camel lactoferrin at 2.7 Å resolution. J. Biol. Chem. 276, 36817-36823 (2001).
145. Khan, J. A., Kumar, P., Sharma, S., Mohanty, A. K., Jabeen, T., Paramasivam, M., Yadav, S., Srinivasan, A. and Singh, T. P. Mechanisms of iron-update and iron-release in lactoferrins. Proc. Ind. Nat. Sci. Acad. B68, 217-234 (2002).
146. Kumar, P., Khan, J. A., Yadav, S. and Singh, T. P. Crystal structure of equine apolactoferrin at 30°C provides further evidence of closed conformations of N- and C-lobes. Acta Cryst. D58, 225-232 (2002).
147. Sharma, S., Jasti, J., Kumar. J., Mohanty, A. K. and Singh, T. P. Crystal structure of a proteolytically generated functional monoferric C-lobe of bovine lactoferrin at 1.9 Å resolution. J. Mol. Biol. 321, 1286-1296 (2003).
148. Jabeen, T., Sharma, S., Singh, N., Bhushan, A. and Singh, T. P. Structure of the zinc-saturated C-terminal half of bovine lactoferrin at 2.0 Å resolution. Acta Cryst. D61, 1107-1115 (2005).
149. Jain, D., Kaur, K. J., Sundaravadivel, B. and Salunke, D. M. Structural and functional consequences of peptidecarbohydrate mimicry: crystal structure of a carbohydrate mimicking peptide bound to concanavalin A. J. Biol Chem. 275, 16098-16102 (2000).
150. Nair, D. T., Singh, K., Sahu, N., Rao, K. V. S. and Salunke, D. M. Crystal structure of an antibody bound to an immunodominant peptide epitope: novel features in peptideantibody recognition. J. Immunol. 165, 6949-6955 (2000).
151. Jain, D., Kaur, K. J. and Salunke, D. M. Plasticity in proteinpeptide recognition: crystal structures of two different peptides bound to concanavalin A. Biophys. J. 80, 2912-2921 (2001).
152. Jain, D., Kaur, K. J. and Salunke, D. M. Enhanced binding of a peptide ligand of concanavalin A arises from improved geometrical complementarity. Biochemistry 40, 12059-12066 (2001).
153. Goel, M., Jain, D., Kaur, K., Kenoth, R., Maiya, B. G., Swamy, M. J. and Salunke, D. M. Functional equality in the absence of structural similarity: an added dimension to molecular mimicry. J. Biol. Chem. 276, 39277-39281 (2001).
154. Jain, D., Nair, D. T., Swaminathan, G. J., Abraham, E. G., Nagaraju, J. and Salunke, D. M. Structure of the induced antibacterial protein from tasar silkworm, Antheraea mylitta: implications to molecular evolution. J. Biol. Chem. 276, 41377-41382 (2001).
155. Nair, D. T., Singh, K., Siddiqui, Z., Nayak, B. P., Rao, K. V. S. and Salunke, D. M. Epitope recognition by diverse antibodies suggests conformational convergence in an antibody response. J. Immunol. 168, 2371-2382 (2002).
156. Goel, M., Anuradha, P., Kaur, K. J., Maiya, B. C., Swamy, M. J. and Salunke, D. M. Porphyrin binding to jacalin is facilitated by the inherent plasticity of the carbohydrate binding site: novel mode of lectin-ligand interaction. Acta Cryst. D60, 281-288 (2004).
157. Goel, M., Damai, R. S., Sethi, D. K., Kaur, K. J., Maiya, B. C., Swamy, M. J. and Salunke, D. M. Crystal structures of PNA-porphyrin complex in the presence and absence of lactose: mapping the conformational changes on lactose binding, interacting surfaces and supramolecular aggregations. Biochemistry 44, 5588-5596 (2005).
158. Sethi, D. K., Agarwal, A., Manivel, V., Rao, K. V. and Salunke, D. M. Differential epitope positioning within the germline antibody paratope enhances promiscuity in the primary immune response. Immunity 24, 429-438 (2006).
159. Krishnan, L., Lomash, S., Raj, B. P., Kaur, K. J. and Salunke, D. M. Paratope plasticity in diverse modes facilitates molecular mimicry in antibody response. J Immunol. 178, 7923-7931 (2007).
160. Pillai, B., Kannan, K. K. and Hosur, M. V. 1.9 Å X-ray study shows closed flap conformation in crystals of tethered HIV-1 protease. Proteins: Struct. Funct. Genet. 43, 57-64 (2001).
161. Kumar, M., Kannan, K. K., Hosur, M. V., Neel, S., Bhavesh, N. S., Chatterjee, A., Mittal, R. and Hosur, R. V. Effects of remote mutation on the autolysis of HIV-I PR: X-ray & NMR investigations. Biochem. Biophy. Res. Commun. 294, 395-401 (2002).
162. Mukesh Kumar and Hosur, M. V. Adaptability and flexibility of HIV-I protease. Eur. J. Biochem. 270, 1231-1239 (2003).
163. Prashar, V. and Hosur, M. V. 1.8 Å X-ray structure of C95M/C1095F double mutant of tethered HIV-1 protease dimer complexed with acetyl pepstatin. Biochem. Biophys. Res. Commun. 323, 1229-1235 (2004).
164. Kumar, M., Prashar, V., Mahale, S. and Hosur, M. V. Observation of a tetrahedral reaction intermediate in the structure of HIV-1 protease substrate complex. Biochem. J. 389, 365-371 (2005).
165. Das, A., Prashar, V., Mahale, S., Serre, L., Ferrer, J. L. & Hosur, M. V. Crystal structure of HIV-1 protease in situ product complex and observation of a low-barrier hydrogen bond between catalytic aspartates. Proc. Natl Acad. Sci. USA 103, 18464-18469 (2006).
166. 2 at 293K: comparison of the effects of sequence and temperature. Acta Cryst. D58, 1381-1384 (2002).
167. Thiyagarajan, S., Rajan, S. S, and Gautham. N. Cobalt hexammine induced tautomeric shift in Z-DNA: the structure of d(CGCGCA).d(TGCGCG) in two crystal forms. Nucleic Acids Res. 32, 5945-5953 (2004).
168. Thiyagarajan, S., Rajan, S. S. and Gautham, N. Structure of d(TGCGCG). d(CGCGCA) in two crystal forms: effect of sequence and crystal packing in Z-DNA. Acta Cryst. D61, 1125-1131 (2005).
169. Suresh, C. G., Pundle, A. V., Rao, K. N., SivaRaman, H., Brannigan, J. A., McVey, C. E., Verma, C. S., Dauter, Z., Dodson, E. J. and Dodson, G. G. Penicillin V acylase crystal structure reveals new Ntn-hydrolase family members. Nat. Struct. Biol. 6, 414-416 (1999).
170. Kumar, R. S., Brannigan, J. A., Prabhune, A. A., Pundle, A. V., Dodson, G. G., Dodson, E. J. and Suresh, C. G. Structural and functional analysis of a conjugated bile salt hydrolase from Bifidobacterium longum reveals an evolutionary relationship with penicillin V acylase. J. Biol. Chem. 281, 32516-32525 (2006).
171. 2. Biochemistry 43, 12477-12488 (2004).
172. Mohanty, A. K., Singh, G., Paramasivam, M., Sarvanan, K., Jabeen, T., Sharma, S., Yadav, S., Kaur, P., Kumar, P., Srinivasan, A. and Singh, T. P. Crystal structure of a new regulatory 40 kDa mammary gland protein (MGP-40) involved in the metastases of patients with recurrent breast cancer. J. Biol. Chem. 278, 14451-14460 (2003).
173. Srivastava, D. B., Ethayathulla, A. S., Kumar, J., Singh, N., Sharma, S., Das, U., Srinivasan, A. and Singh, T. P. Crystal structure of a secretory signalling glycoprotein from sheep at 2.0 Å resolution. J. Struct. Biol. 156, 505-516 (2006).
174. Kumar, J., Ethayathulla, A. S., Srivastava, D. B., Sharma, S., Singh, S. B., Srinivasan, A., Yadav, M. P. and Singh, T. P. Structure of a bovine secretory signalling glycoprotein (SPC-40) at 2.1 Å resolution. Acta Cryst D62, 953-963 (2006).
175. Srivastava, D. B., Ethayathulla, A. S., Kumar, J., Somvanshi, R. K., Sharma, S., Dey, S. and Singh, T. P. Carbohydrate binding properties and carbohydrate induced conformational switch in sheep secretory glycoprotein (SPS-40): crystal structures of four complexes of SPS-40 with chitin-like oligosaccharides. J. Struct. Biol. 158, 255-266 (2007).
176. Kumar, J., Ethayathulla, A. S., Srivastava, D. B., Singh, N., Sharma, S., Kaur, P., Srinivasan, A. and Singh, T. P. Carbohydrate-binding properties of goat secretory glycoprotein (SPG-40) and its functional implications: structures of the native glycoprotein and its four complexes with chitin-like oligosaccharides. Acta Cryst. D63, 437-446 (2007).
177. Dwivedi, S., Kruparani, S. P. and Sankaranarayanan, R. A Damino acid editing module coupled to the translational apparatus in archaea. Nat Struct. Mol. Biol. 12, 556-557 (2005).
178. Datta, A. B., Panjikar, S., Weiss, M. S., Chakrabarti, P. and Parrack, P. Structure of λ CII: implications for recognition of direct-repeat DNA by an unusual tetrameric organization. Proc. Natl. Acad. Sci. USA 102, 11242-11247 (2005).
179. 2. J. Mol. Biol. 324, 755-762 (2002).
180. Sekar, K., Vaijayanthi Mala, S., Yogavel, M., Velmurugan, D., Poi, M.-J., Vishwanath, B. S., Gowda, T.V., Jeyaprakash, A. A. and Tsai, M.-D. Crystal structures of the free and anisic acid bound triple mutant of phospholipase. J. Mol. Biol. 333, 367-376 (2003).
181. Sekar, K. Structural biology of recombinant bovine pancreatic phospholipase A2 and its inhibitor complexes. Curr. Top. Med. Chem. 7, 779-785 (2007).
182. Girish, T. S. and Gopal, B. The crystal structure of the catalytic domain of the chick retinal neurite inhibitor-receptor protein tyrosine phosphatase CRYP-2/cPTPRO. Proteins: Struct. Func. Bioinf. [Epub].
183. 4: implications for decreased ATPase activity and molecular aggregation. Nucleic Acids Res. 28, 4964-4973 (2000).
184. Datta, S., Ganesh, N., Chandra, N. R., Muniyappa, K. and Vijayan, M. Structural studies on MtRecA-nudeotide complexes: insights into DNA and nucleotide binding and the structural signature of NTP recognition. Proteins: Struct. Funct. Genet 50, 474-485 (2003).
185. Datta, S., Krishna, R., Ganesh, N., Chandra, N. R., Muniyappa, K. and Vijayan, M. Crystal structures of Mycobaderium smegmatis RecA and its nucleotide complexes. J. Bacteriol. 185, 4280-4284 (2003).
186. Krishna, R., Manjunath, G. P., Kumar, P., Surolia, A., Chandra, N. R., Muniyappa, K. and Vijayan, M. Crystallographic identification of an ordered C-terminal domain and a second nucleotide-binding site in RecA: new insights into allostery. Nucleic Acids Res. 34, 2186-2195 (2006).
187. Krishna, R., Prabu, J. R., Manjunath, G. P., Datta, S., Chandra, N. R., Muniyappa, K. and Vijayan, M. Snapshots of RecA protein involving movement of the C-domain and different conformations of the DNA-binding loops: crystallographic and comparative analysis of 11 structures of Mycobaderium smegmatis RecA. J. Mol. Biol. 367, 1130-1144 (2007).
188. Saikrishnan, K., Jeyakanthan, J., Venkatesh, J., Acharya, N., Sekar, K., Varshney, U. and Vijayan, M. Structure of Mycobacterium tuberculosis single-stranded DNA-binding protein. Variability in quaternary structure and its implications. J. Mol. Biol. 331, 385-393 (2003).
189. Saikrishnan, K., Manjunath, G. P., Singh Pawan, Jeyakanthan, J., Dauter, Z., Sekar, K., Muniyappa, K. and Vijayan, M. Structure of Mycobaderium smegmatis single-stranded DNA-binding protein and a comparative study involving homologus SSBs: biological implications of structural plasticity and variability in quaternary association. Acta Cryst D61, 1140-1148 (2005).
190. Saikrishnan, K., Kalapala, S. K., Varshney, U. and Vijayan, M. X-ray structural studies of Mycobaderium tuberculosis RRF and a comparative study of RRFs of known structure. Molecular plasticity and biological implications. J. Mol. Biol. 345, 29-38 (2005).
191. Das, S., Kumar, P., Bhor, V., Surolia, A. and Vijayan, M. Invariance and variability in bacterial PanK: a study based on the crystal structure of Mycobacterium tuberculosis PanK. Acta Cryst. D62, 628-638 (2006).
192. Roy, S., Gupta, S., Das, S., Sekar, K., Chatterji, D. and Vijayan, M. X-ray analysis of Mycobaderium smegmatis Dps and a comparative study involving other Dps and Dpslike molecules. J. Mol. Biol. 339, 1103-1113 (2004).
193. Roy, S., Saraswathi, R., Gupta, S., Sekar, K., Chatterji, D. and Vijayan, M. Role of N and C-terminal tails in DNA binding and assembly in Dps: structural studies of Mycobaderium smegmatis Dps deletion mutants. J. Mol. Biol. 370, 752-767 (2007).
194. Ketkar, A. D., Shenoy, A. R., Ramagopal, U. A., Visweswariah, S. S., Suguna, K. A structural basis for the role of nucleotide specifying residues in regulating the oligomerization of the Rv1625c adenylyl cydase from M. tuberculosis. J. Mol. Biol. 356, 904-916 (2006).
195. C from Mycobaderium tuberculosis. J. Biol. Chem. 282, 4711-4718 (2007).
196. Taneja, B. and Mande, S. C. Structure of Mycobacterium tuberculosis chaperonin-10 at 3.5Å resolution. Acta Cryst. D58, 260-266 (2002).
197. Qamra, R. and Mande, S. C. Crystal structure of the 65 kDa heat shock protein, chaperonin 60.2 of Mycobacterium tuberculosis. J. Bacteriol. 186, 8105-8113 (2004).
198. Akif, M., Suhre, K., Verma, C. and Mande, S. C. Conformational flexibility of Mycobaderium tuberculosis thioredoxin reductase: crystal structure and normal-mode analysis. Acta Cryst. D61, 1603-1611 (2005).
199. Qamra, R., Prakash, P., Aruna, B., Hasnain, S. E. and Mande, S. C. The 2.15 Å crystal structure of Mycobaderium tuberculosis chorismate mutase reveals an unexpected gene duplication and suggests a role in host-pathogen interactions. Biochemistry 45, 6997-7005 (2006).
200. Gupta, A., Kumar, P. H., Dineshkumar, T. K., Varshney, U. and Subramanya, H. S. Crystal structure of Rv2118c: an AdoMet dependent methyltransferase from Mycobacterium tuberculosis H37Rv. J. Mol. Biol. 312, 381-391 (2001).
201. +- dependent DNA ligase (rv3014c) from M. tuberculosis: crystal structure of the adenylation domain and identification of novel inhibitors. J. Biol. Chem. 280, 30273-30281 (2005).
202. +-dependent DNA ligase is selectively inhibited by glycosylamines compared with human DNA ligase I. Nucleic Acids Res. 33, 7090-7101 (2005).
203. Tripathi, S. M. and Ramachandran, R. Direct evidence for a glutamate switch necessary for substrate recognition: crystal structures of lysine epsilon-aminotransferase (Rv3290c) from Mycobaderium tuberculosis H37Rv. J. Mol. Biol. 362, 877-886 (2006).
204. Sankaranarayanan, R., Saxena, P., Marathe, U., Gokhale, R. S., Shanmugam, V. M. and Rukmini, R. A novel tunnel in mycobacterial type III polyketide synthase reveals the structural basis for generating diverse metabolites. Nat. Struct. Mol. Biol. 11, 894-900 (2004).
205. Chaithanya, M., Rajakumara, E., Mazumdar, P., Saha, B., Mitra, D., Wiker, H. G., Sankaranarayanan, R. and Das, A. K. Crystal structure of low molecular-weight protein tyrosine phosphatase from Mycobacterium tuberculosis at 1.9-Å Resolution. J. Bacteriol. 187, 2175-2181 (2005).
206. Simanshu, D. K., Savithri, H. S. and Murthy, M. R. N. Crystal structures of ADP and AMPPNP bound propionate kinase (TdcD) from Salmonella typhimurium: comparison with members of acetate and sugar kinase / heat shock cognate 70 / actin superfamily. J. Mol. Biol. 352, 876-892 (2005).
207. Simanshu, D. K., Savithri, H. S. and Murthy, M. R. N. Crystal structures of Salmonella typhimurium biodegradative threonine deaminase and its complex with CMP provide structural insights into ligand-induced oligomerization and enzyme activation. J. Biol. Chem. 281, 39630-39641 (2006).
208. Chittori, S., Simanshu, D. K., Savithri, H. S. and Murthy, M. R. N. Structure of the putative mutarotase YeaD from Salmonella typhimurium: structural comparison with galactose mutarotases. Acta Cryst. D63, 197-205 (2007).
209. Deepa, R., Durga Rao, C. and Suguna, K. Structure of the extended diarrhea-inducing domain of rotavirus enterotoxigenic protein NSP4. Arch Virol. 152, 847-859 (2007).
210. Velankar, S. S., Ray, S. S., Gokhale, R. S., Suma, S., Balaram, H., Balaram, P. and Murthy, M. R. N. Triose phosphate isomerase from Plasmodium falciparum: the crystal structure provides insights into antimalarial drug design. Structure 5, 751-761 (1997).
211. Gopal, B., Ray, S. S., Gokhale, R. S., Balaram, H., Murthy, M. R. N. and Balaram, P. Cavity creating mutation at dimer interface of Plasmodium falciparum and restoration of stability by disulfide cross linking of subunits. Biochemistry 38, 478-486 (1999).
212. Parthasarathy, S., Balaram, H., Balaram, P. and Murthy, M. R. N. Structure of Plasmodium falciparum triosephosphate isomerase- phosphoglycolate complex in two crystal forms: characterization of catalytic loop in open and closed conformation in the ligand bound state. Biochemistry 41, 13178-13188 (2002).
213. Parthasarathy, S., Balaram, H., Balaram, P. and Murthy, M. R. N. Structures of Plasmodium falciparum triosephosphate isomerase complexed to substrate analogues: observation of the catalytic loop in the open conformation in the ligand-bound state. Acta Cryst. D58, 1992-2000 (2002).
214. Parthasarathy, S., Eaazhisai, K., Balaram, H., Balaram, P. and Murthy, M. R. N. Structure of Plasmodium falciparum TIM-2-phosphoglycerate complex at 1.1Å resolution. J. Biol. Chem. 278, 52461-52470 (2003).
215. Eaazhisai, K., Jayalakshmi, R., Gayathri, P., Anand, R. P., Sumathy, K., Balaram, H. and Murthy, M. R. N. Crystal Structure of fully ligated Adenylosuccinate synthetase from Plasmodium falciparum. J. Mol. Biol. 335, 1251-1264 (2004).
216. Pidugu, L. S., Kapoor, M., Surolia, N., Surolia, A. and Suguna, K. Structural basis for the variation in triclosan affinity to enoyl reductases. J. Mol. Biol. 343, 147-155 (2004).
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