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Volumn 473, Issue 9, 2016, Pages 1267-1280

Exploring the structure of glutamate racemase from Mycobacterium tuberculosis as a template for anti-mycobacterial drug discovery

Author keywords

Analytical ultracentrifugation; Enzyme kinetics; Glutamate racemase; Monomer engineering; Mycobacterium tuberculosis; Thermofluor.

Indexed keywords

ANTIMYCOBACTERIAL AGENT; GLUTAMATE RACEMASE; RACEMASE; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; GLUTAMIC ACID; ISOMERASE;

EID: 84975105974     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BCJ20160186     Document Type: Article
Times cited : (20)

References (63)
  • 1
    • 33947511253 scopus 로고    scopus 로고
    • The TB pandemic: An old problem seeking new solutions
    • CrossRef PubMed
    • Meya, D.B. and McAdam, K.P. (2007) The TB pandemic: an old problem seeking new solutions. J. Intern. Med. 261, 309-329 CrossRef PubMed
    • (2007) J. Intern. Med , vol.261 , pp. 309-329
    • Meya, D.B.1    McAdam, K.P.2
  • 3
    • 13844319812 scopus 로고    scopus 로고
    • The magic bullets and tuberculosis drug targets
    • CrossRef PubMed
    • Zhang, Y. (2005) The magic bullets and tuberculosis drug targets. Annu. Rev. Pharmacol. Toxicol. 45, 529-564 CrossRef PubMed
    • (2005) Annu. Rev. Pharmacol. Toxicol , vol.45 , pp. 529-564
    • Zhang, Y.1
  • 4
  • 5
    • 58949092833 scopus 로고    scopus 로고
    • Glutamate racemase as a target for drug discovery
    • CrossRef PubMed
    • Fisher, S.L. (2008) Glutamate racemase as a target for drug discovery. Microb. Biotechnol. 1, 345-360 CrossRef PubMed
    • (2008) Microb. Biotechnol , vol.1 , pp. 345-360
    • Fisher, S.L.1
  • 6
    • 0034762821 scopus 로고    scopus 로고
    • Recent advances in the formation of the bacterial peptidoglycan monomer unit
    • CrossRef PubMed
    • van Heijenoort, J. (2001) Recent advances in the formation of the bacterial peptidoglycan monomer unit. Nat. Prod. Rep. 18, 503-519 CrossRef PubMed
    • (2001) Nat. Prod. Rep , vol.18 , pp. 503-519
    • Van Heijenoort, J.1
  • 7
    • 0001210324 scopus 로고
    • Transamination of D-amino acids by Bacillus subtilis
    • PubMed
    • Thorne, C.B., Gomez, C.G. and Housewright, R.D. (1955) Transamination of D-amino acids by Bacillus subtilis. J. Bacteriol. 69, 357-362 PubMed
    • (1955) J. Bacteriol , vol.69 , pp. 357-362
    • Thorne, C.B.1    Gomez, C.G.2    Housewright, R.D.3
  • 8
    • 0001398484 scopus 로고
    • D-Amino acid transamination in Bacillus anthracis
    • PubMed
    • Thorne, C.B. and Molnar, D.M. (1955) D-Amino acid transamination in Bacillus anthracis. J. Bacteriol. 70, 420-426 PubMed
    • (1955) J. Bacteriol , vol.70 , pp. 420-426
    • Thorne, C.B.1    Molnar, D.M.2
  • 9
    • 33750976703 scopus 로고    scopus 로고
    • Glutamate racemase from Mycobacterium tuberculosis inhibits DNA gyrase by affecting its DNA-binding
    • CrossRef PubMed
    • Sengupta, S., Shah, M. and Nagaraja, V. (2006) Glutamate racemase from Mycobacterium tuberculosis inhibits DNA gyrase by affecting its DNA-binding. Nucleic Acids Res 34, 5567-5576 CrossRef PubMed
    • (2006) Nucleic Acids Res , vol.34 , pp. 5567-5576
    • Sengupta, S.1    Shah, M.2    Nagaraja, V.3
  • 11
    • 84920364934 scopus 로고    scopus 로고
    • Revisiting the essentiality of glutamate racemase in Mycobacterium tuberculosis
    • CrossRef PubMed
    • Morayya, S., Awasthy, D., Yadav, R., Ambady, A. and Sharma, U. (2015) Revisiting the essentiality of glutamate racemase in Mycobacterium tuberculosis. Gene 555, 269-276 CrossRef PubMed
    • (2015) Gene 555 , pp. 269-276
    • Morayya, S.1    Awasthy, D.2    Yadav, R.3    Ambady, A.4    Sharma, U.5
  • 12
    • 84914142689 scopus 로고    scopus 로고
    • Investigation of the essentiality of glutamate racemase in Mycobacterium smegmatis
    • CrossRef PubMed
    • Li, Y., Mortuza, R., Milligan, D.L., Tran, S.L., Strych, U., Cook, G.M. and Krause, K.L. (2014) Investigation of the essentiality of glutamate racemase in Mycobacterium smegmatis. J. Bacteriol. 196, 4239-4244 CrossRef PubMed
    • (2014) J. Bacteriol , vol.196 , pp. 4239-4244
    • Li, Y.1    Mortuza, R.2    Milligan, D.L.3    Tran, S.L.4    Strych, U.5    Cook, G.M.6    Krause, K.L.7
  • 14
    • 0032915050 scopus 로고    scopus 로고
    • Structure and mechanism of glutamate racemase from Aquifex pyrophilus
    • CrossRef PubMed
    • Hwang, K.Y., Cho, C.S., Kim, S.S., Sung, H.C., Yu, Y.G. and Cho, Y. (1999) Structure and mechanism of glutamate racemase from Aquifex pyrophilus. Nat. Struct. Biol. 6, 422-426 CrossRef PubMed
    • (1999) Nat. Struct. Biol , vol.6 , pp. 422-426
    • Hwang, K.Y.1    Cho, C.S.2    Kim, S.S.3    Sung, H.C.4    Yu, Y.G.5    Cho, Y.6
  • 15
    • 27644453362 scopus 로고    scopus 로고
    • Substrate-induced conformational changes in Bacillus subtilis glutamate racemase and their implications for drug discovery
    • CrossRef PubMed
    • Ruzheinikov, S.N., Taal, M.A., Sedelnikova, S.E., Baker, P.J. and Rice, D.W. (2005) Substrate-induced conformational changes in Bacillus subtilis glutamate racemase and their implications for drug discovery. Structure 13, 1707-1713 CrossRef PubMed
    • (2005) Structure , vol.13 , pp. 1707-1713
    • Ruzheinikov, S.N.1    Taal, M.A.2    Sedelnikova, S.E.3    Baker, P.J.4    Rice, D.W.5
  • 16
    • 34547557316 scopus 로고    scopus 로고
    • Structural and functional analysis of two glutamate racemase isozymes from Bacillus anthracis and implications for inhibitor design
    • CrossRef PubMed
    • May, M., Mehboob, S., Mulhearn, D.C., Wang, Z., Yu, H., Thatcher, G.R., Santarsiero, B.D., Johnson, M.E. and Mesecar, A.D. (2007) Structural and functional analysis of two glutamate racemase isozymes from Bacillus anthracis and implications for inhibitor design. J. Mol. Biol. 371, 1219-1237 CrossRef PubMed
    • (2007) J. Mol. Biol , vol.371 , pp. 1219-1237
    • May, M.1    Mehboob, S.2    Mulhearn, D.C.3    Wang, Z.4    Yu, H.5    Thatcher, G.R.6    Santarsiero, B.D.7    Johnson, M.E.8    Mesecar, A.D.9
  • 17
    • 34547932250 scopus 로고    scopus 로고
    • Structural basis for glutamate racemase inhibition
    • CrossRef PubMed
    • Kim, K., Bong, Y.J., Park, J.K., Shin, K.J., Hwang, K.Y. and Kim, E.E. (2007) Structural basis for glutamate racemase inhibition. J. Mol. Biol. 372, 434-443 CrossRef PubMed
    • (2007) J. Mol. Biol , vol.372 , pp. 434-443
    • Kim, K.1    Bong, Y.J.2    Park, J.K.3    Shin, K.J.4    Hwang, K.Y.5    Kim, E.E.6
  • 19
    • 0027155359 scopus 로고
    • Isotope effects and the identification of catalytic residues in the reaction catalyzed by glutamate racemase
    • CrossRef PubMed
    • Tanner, M.E., Gallo, K.A. and Knowles, J.R. (1993) Isotope effects and the identification of catalytic residues in the reaction catalyzed by glutamate racemase. Biochemistry 32, 3998-4006 CrossRef PubMed
    • (1993) Biochemistry , vol.32 , pp. 3998-4006
    • Tanner, M.E.1    Gallo, K.A.2    Knowles, J.R.3
  • 20
    • 0027212678 scopus 로고
    • The murI gene of Escherichia coli is an essential gene that encodes a glutamate racemase activity
    • PubMed
    • Doublet, P., van Heijenoort, J., Bohin, J.P. and Mengin-Lecreulx, D. (1993) The murI gene of Escherichia coli is an essential gene that encodes a glutamate racemase activity. J. Bacteriol. 175, 2970-2979 PubMed
    • (1993) J. Bacteriol. , vol.175 , pp. 2970-2979
    • Doublet, P.1    Van Heijenoort, J.2    Bohin, J.P.3    Mengin-Lecreulx, D.4
  • 21
    • 0037179637 scopus 로고    scopus 로고
    • 4-Substituted D-glutamic acid analogues: The first potent inhibitors of glutamate racemase (MurI) enzyme with antibacterial activity
    • CrossRef PubMed
    • de Dios, A., Prieto, L., Martin, J.A., Rubio, A., Ezquerra, J., Tebbe, M., Lopez de Uralde, B., Martin, J., Sanchez, A., LeTourneau, D.L. et al. (2002) 4-Substituted D-glutamic acid analogues: the first potent inhibitors of glutamate racemase (MurI) enzyme with antibacterial activity. J. Med. Chem. 45, 4559-4570 CrossRef PubMed
    • (2002) J. Med. Chem , vol.45 , pp. 4559-4570
    • De Dios, A.1    Prieto, L.2    Martin, J.A.3    Rubio, A.4    Ezquerra, J.5    Tebbe, M.6    Lopez De Uralde, B.7    Martin, J.8    Sanchez, A.9    LeTourneau, D.L.10
  • 22
    • 48849113288 scopus 로고    scopus 로고
    • Design of Helicobacter pylori glutamate racemase inhibitors as selective antibacterial agents: A novel pro-drug approach to increase exposure
    • CrossRef PubMed
    • Basarab, G.S., Hill, P.J., Rastagar, A. and Webborn, P.J. (2008) Design of Helicobacter pylori glutamate racemase inhibitors as selective antibacterial agents: A novel pro-drug approach to increase exposure. Bioorg. Med. Chem. Lett. 18, 4716-4722 CrossRef PubMed
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , pp. 4716-4722
    • Basarab, G.S.1    Hill, P.J.2    Rastagar, A.3    Webborn, P.J.4
  • 25
    • 77956645841 scopus 로고    scopus 로고
    • Exploiting enzyme plasticity in virtual screening: High efficiency inhibitors of glutamate racemase
    • CrossRef PubMed
    • Whalen, K.L., Pankow, K.L., Blanke, S.R. and Spies, MA. (2010) Exploiting enzyme plasticity in virtual screening: high efficiency inhibitors of glutamate racemase. ACS Med. Chem. Lett. 1, 9-13CrossRef PubMed
    • (2010) ACS Med. Chem. Lett. , vol.1 , pp. 9-13
    • Whalen, K.L.1    Pankow, K.L.2    Blanke, S.R.3    Spies, M.A.4
  • 27
    • 0034711265 scopus 로고    scopus 로고
    • Self-association of human apolipoprotein E3 and E4 in the presence and absence of phospholipid
    • CrossRef PubMed
    • Perugini, M.A., Schuck, P. and Howlett, G.J. (2000) Self-association of human apolipoprotein E3 and E4 in the presence and absence of phospholipid. J. Biol. Chem. 275, 36758-36765 CrossRef PubMed
    • (2000) J. Biol. Chem , vol.275 , pp. 36758-36765
    • Perugini, M.A.1    Schuck, P.2    Howlett, G.J.3
  • 28
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling
    • CrossRef PubMed
    • Schuck, P. (2000) Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling. Biophys. J. 78, 1606-1619 CrossRef PubMed
    • (2000) Biophys J. , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 29
    • 0036154258 scopus 로고    scopus 로고
    • Size-distribution analysis of proteins by analytical ultracentrifugation: Strategies and application to model systems
    • CrossRef PubMed
    • Schuck, P., Perugini, M.A., Gonzales, N.R., Howlett, G.J. and Schubert, D. (2002) Size-distribution analysis of proteins by analytical ultracentrifugation: strategies and application to model systems. Biophys. J. 82, 1096-1111 CrossRef PubMed
    • (2002) Biophys J , vol.82 , pp. 1096-1111
    • Schuck, P.1    Perugini, M.A.2    Gonzales, N.R.3    Howlett, G.J.4    Schubert, D.5
  • 30
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • CrossRef
    • Kabsch, W. (1993) Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 26, 795-800 CrossRef
    • (1993) J. Appl. Crystallogr , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 31
    • 0036111645 scopus 로고    scopus 로고
    • The computational crystallography toolbox: Crystallographic algorithms in a reusable software framework
    • CrossRef
    • Grosse-Kunstleve, R.W., Sauter, N.K., Moriarty, N.W. and Adams, P.D. (2002) The computational crystallography toolbox: crystallographic algorithms in a reusable software framework. J. Appl. Crystallogr. 35, 126-136 CrossRef
    • (2002) J. Appl. Crystallogr , vol.35 , pp. 126-136
    • Grosse-Kunstleve, R.W.1    Sauter, N.K.2    Moriarty, N.W.3    Adams, P.D.4
  • 32
    • 33644875355 scopus 로고    scopus 로고
    • Scaling and assessment of data quality
    • CrossRef PubMed
    • Evans, P. (2006) Scaling and assessment of data quality. Acta Crystallogr. D Biol. Crystallogr. 62, 72-82 CrossRef PubMed
    • (2006) Acta Crystallogr. D Biol. Crystallogr , vol.62 , pp. 72-82
    • Evans, P.1
  • 34
    • 0033213239 scopus 로고    scopus 로고
    • The finer things in X-ray diffraction data collection
    • CrossRef PubMed
    • Pflugrath, J.W. (1999) The finer things in X-ray diffraction data collection. Acta Crystallogr. D Biol. Crystallogr. 55, 1718-1725 CrossRef PubMed
    • (1999) Acta Crystallogr. D Biol. Crystallogr , vol.55 , pp. 1718-1725
    • Pflugrath, J.W.1
  • 36
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • CrossRef PubMed
    • Matthews, B.W. (1968) Solvent content of protein crystals. J. Mol. Biol. 33, 491-497 CrossRef PubMed
    • (1968) J. Mol. Biol , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 39
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • CrossRef PubMed
    • Emsley, P. and Cowtan, K. (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60, 2126-2132 CrossRef PubMed
    • (2004) Acta Crystallogr. D Biol. Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 41
    • 3242886389 scopus 로고    scopus 로고
    • MolProbity: Structure validation and all-atom contact analysis for nucleic acids and their complexes
    • CrossRef PubMed
    • Davis, I.W., Murray, L.W., Richardson, J.S. and Richardson, D.C. (2004) MolProbity: structure validation and all-atom contact analysis for nucleic acids and their complexes. Nucleic. Acids Res. 32, W615-W619 CrossRef PubMed
    • (2004) Nucleic. Acids Res , vol.32 , pp. W615-W619
    • Davis, I.W.1    Murray, L.W.2    Richardson, J.S.3    Richardson, D.C.4
  • 42
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • CrossRef PubMed
    • Krissinel, E. and Henrick, K. (2004) Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr. D Biol. Crystallogr. 60, 2256-2268 CrossRef PubMed
    • (2004) Acta Crystallogr. D Biol. Crystallogr , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 44
    • 65449188232 scopus 로고    scopus 로고
    • Jalview version 2-a multiple sequence alignment editor and analysis workbench
    • CrossRef PubMed
    • Waterhouse, A.M., Procter, J.B., Martin, D.M., Clamp, M. and Barton, G.J. (2009) Jalview version 2-a multiple sequence alignment editor and analysis workbench. Bioinformatics 25, 1189-1191 CrossRef PubMed
    • (2009) Bioinformatics , vol.25 , pp. 1189-1191
    • Waterhouse, A.M.1    Procter, J.B.2    Martin, D.M.3    Clamp, M.4    Barton, G.J.5
  • 45
    • 58149187898 scopus 로고    scopus 로고
    • PDBsum new things
    • CrossRef PubMed
    • Laskowski, R.A. (2009) PDBsum new things. Nucleic. Acids Res. 37, D355-D339 CrossRef PubMed
    • (2009) Nucleic. Acids Res , vol.37 , pp. D355-D1339
    • Laskowski, R.A.1
  • 46
    • 0035964342 scopus 로고    scopus 로고
    • Electrostatics of nanosystems: Application to microtubules and the ribosome
    • U. S. A CrossRef PubMed
    • Baker, N.A., Sept, D., Joseph, S., Holst, M.J. and McCammon, J.A. (2001) Electrostatics of nanosystems: application to microtubules and the ribosome. Proc. Natl. Acad. Sci. U.S.A. 98, 10037-10041 CrossRef PubMed
    • (2001) Proc. Natl. Acad. Sci. , vol.98 , pp. 10037-10041
    • Baker, N.A.1    Sept, D.2    Joseph, S.3    Holst, M.J.4    McCammon, J.A.5
  • 47
    • 3242886771 scopus 로고    scopus 로고
    • PDB2PQR: An automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations
    • CrossRef PubMed
    • Dolinsky, T.J., Nielsen, J.E., McCammon, J.A. and Baker, N.A. (2004) PDB2PQR: an automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations. Nucleic. Acids Res. 32, W665-W667 CrossRef PubMed
    • (2004) Nucleic. Acids Res , vol.32 , pp. W665-W667
    • Dolinsky, T.J.1    Nielsen, J.E.2    McCammon, J.A.3    Baker, N.A.4
  • 48
    • 84860392201 scopus 로고    scopus 로고
    • An efficient one-step site-directed deletion, insertion, single and multiple-site plasmid mutagenesis protocol
    • CrossRef PubMed
    • Liu, H. and Naismith, J.H. (2008) An efficient one-step site-directed deletion, insertion, single and multiple-site plasmid mutagenesis protocol. BMC Biotechnol. 8, 1-10 CrossRef PubMed
    • (2008) BMC Biotechnol , vol.8 , pp. 1-10
    • Liu, H.1    Naismith, J.H.2
  • 49
    • 0033616629 scopus 로고    scopus 로고
    • Catalytic acid/base residues of glutamate racemase
    • CrossRef PubMed
    • Glavas, S. and Tanner, M.E. (1999) Catalytic acid/base residues of glutamate racemase. Biochemistry 38, 4106-4113 CrossRef PubMed
    • (1999) Biochemistry , vol.38 , pp. 4106-4113
    • Glavas, S.1    Tanner, M.E.2
  • 50
    • 0035967535 scopus 로고    scopus 로고
    • Active site residues of glutamate racemase
    • CrossRef PubMed
    • Glavas, S. and Tanner, M.E. (2011) Active site residues of glutamate racemase. Biochemistry 40, 6199-6204 CrossRef PubMed
    • (2011) Biochemistry , vol.40 , pp. 6199-6204
    • Glavas, S.1    Tanner, M.E.2
  • 51
    • 0027263160 scopus 로고
    • Purification, cloning, and cofactor independence of glutamate racemase from Lactobacillus
    • CrossRef PubMed
    • Gallo, K.A. and Knowles, J.R. (1993) Purification, cloning, and cofactor independence of glutamate racemase from Lactobacillus. Biochemistry 32, 3981-3990 CrossRef PubMed
    • (1993) Biochemistry , vol.32 , pp. 3981-3990
    • Gallo, K.A.1    Knowles, J.R.2
  • 52
    • 0028198913 scopus 로고
    • The glutamate racemase activity from Escherichia coli is regulated by peptidoglycan precursor UDP-N-acetylmuramoyl-L-alanine
    • CrossRef PubMed
    • Doublet, P., van Heijenoort, J. and Mengin-Lecreulx, D. (1994) The glutamate racemase activity from Escherichia coli is regulated by peptidoglycan precursor UDP-N-acetylmuramoyl-L-alanine. Biochemistry 33, 5285-5290 CrossRef PubMed
    • (1994) Biochemistry , vol.33 , pp. 5285-5290
    • Doublet, P.1    Van Heijenoort, J.2    Mengin-Lecreulx, D.3
  • 53
    • 0028899510 scopus 로고
    • UDP-N-acetylmuramyl-L-alanine functions as an activator in the regulation of the Escherichia coli glutamate racemase activity
    • Ho, H.T., Falk, P.J., Ervin, K.M., Krishnan, B.S., Discotto, L.F., Dougherty, T.J. and Pucci, M.J. (1995) UDP-N-acetylmuramyl-L-alanine functions as an activator in the regulation of the Escherichia coli glutamate racemase activity. Biochemistry 34, 2464-2470 CrossRef PubMed
    • (1995) Biochemistry , vol.34 , pp. 2464-2470
    • Ho, H.T.1    Falk, P.J.2    Ervin, K.M.3    Krishnan, B.S.4    Discotto, L.F.5    Dougherty, T.J.6    Pucci, M.J.7
  • 54
    • 67651213699 scopus 로고    scopus 로고
    • Glutamate racemase dimerization inhibits dynamic conformational flexibility and reduces catalytic rates
    • Mehboob, S., Guo, L., Fu, W., Mittal, A., Yau, T., Truong, K., Johlfs, M., Long, F., Fung, L.W. and Johnson, M.E. (2009) Glutamate racemase dimerization inhibits dynamic conformational flexibility and reduces catalytic rates. Biochemistry 48, 7045-7055 CrossRef PubMed
    • (2009) Biochemistry , vol.48 , pp. 7045-7055
    • Mehboob, S.1    Guo, L.2    Fu, W.3    Mittal, A.4    Yau, T.5    Truong, K.6    Johlfs, M.7    Long, F.8    Fung, L.W.9    Johnson, M.E.10
  • 55
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel, E. and Henrick, K. (2007) Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372, 774-797 CrossRef PubMed
    • (2007) J. Mol. Biol , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 56
    • 0030028728 scopus 로고    scopus 로고
    • Principles of protein-protein interactions
    • Jones, S. and Thornton, J.M. (1996) Principles of protein-protein interactions. Proc. Natl. Acad. Sci. U.S.A. 93, 13-20 CrossRef PubMed
    • (1996) Proc. Natl. Acad. Sci. U. S. A , vol.93 , pp. 13-20
    • Jones, S.1    Thornton, J.M.2
  • 57
    • 0030068478 scopus 로고    scopus 로고
    • Identification of the Serratia endonuclease dimer: Structural basis and implications for catalysis
    • Miller, M.D. and Krause, K.L. (1996) Identification of the Serratia endonuclease dimer: structural basis and implications for catalysis. Protein Sci. 5, 24-33 CrossRef PubMed
    • (1996) Protein Sci , vol.5 , pp. 24-33
    • Miller, M.D.1    Krause, K.L.2
  • 58
    • 0242299201 scopus 로고    scopus 로고
    • Dissecting subunit interfaces in homodimeric proteins
    • Bahadur, R.P., Chakrabarti, P., Rodier, F. and Janin, J. (2003) Dissecting subunit interfaces in homodimeric proteins. Proteins 53, 708-719 CrossRef PubMed
    • (2003) Proteins , vol.53 , pp. 708-719
    • Bahadur, R.P.1    Chakrabarti, P.2    Rodier, F.3    Janin, J.4
  • 59
    • 1042275583 scopus 로고    scopus 로고
    • A dissection of specific and non-specific protein-protein interfaces
    • Bahadur, R.P., Chakrabarti, P., Rodier, F. and Janin, J. (2004) A dissection of specific and non-specific protein-protein interfaces. J. Mol. Biol. 336, 943-955 CrossRef PubMed
    • (2004) J. Mol. Biol , vol.336 , pp. 943-955
    • Bahadur, R.P.1    Chakrabarti, P.2    Rodier, F.3    Janin, J.4
  • 62
    • 37349126709 scopus 로고    scopus 로고
    • Inhibition of DNA gyrase activity by Mycobacterium smegmatis MurI
    • Sengupta, S. and Nagaraja, V. (2008) Inhibition of DNA gyrase activity by Mycobacterium smegmatis MurI. FEMS Microbiol. Lett. 279, 40-47 CrossRef PubMed
    • (2008) FEMS Microbiol. Lett. , vol.279 , pp. 40-47
    • Sengupta, S.1    Nagaraja, V.2
  • 63
    • 53449086920 scopus 로고    scopus 로고
    • Moonlighting function of glutamate racemase from Mycobacterium tuberculosis: Racemization and DNA gyrase inhibition are two independent activities of the enzyme
    • Sengupta,S. Ghosh,S. Nagaraja,V.2008Moonlighting function of glutamate racemase from Mycobacterium tuberculosis: Racemization and DNA gyrase inhibition are two independent activities of the enzymeMicrobiology1542796-2803
    • (2008) Microbiology , vol.154 , pp. 2796-2803
    • Sengupta, S.1    Ghosh, S.2    Nagaraja, V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.