메뉴 건너뛰기




Volumn 16, Issue 7, 2007, Pages 1360-1367

Crystal structures of TM0549 and NE1324 - Two orthologs of E. coli AHAS isozyme III small regulatory subunit

Author keywords

Acetohydroxyacid synthase; ACT domain; Actolactate synthase; AHAS; Protein refolding; Regulatory subunit

Indexed keywords

ACETOLACTATE SYNTHASE; AMINO ACID; CALCIUM ION; FERREDOXIN; ISOENZYME; POLYPEPTIDE; SELENOMETHIONINE;

EID: 34250900543     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.072793807     Document Type: Article
Times cited : (18)

References (48)
  • 1
    • 0037466513 scopus 로고    scopus 로고
    • The effects of arginine on refolding of aggregated proteins: Not facilitate refolding, but suppress aggregation
    • Arakawa, T. and Tsumoto, K. 2003. The effects of arginine on refolding of aggregated proteins: Not facilitate refolding, but suppress aggregation. Biochem. Biophys. Res. Commun. 304: 148-152.
    • (2003) Biochem. Biophys. Res. Commun , vol.304 , pp. 148-152
    • Arakawa, T.1    Tsumoto, K.2
  • 2
    • 0033574503 scopus 로고    scopus 로고
    • Gleaning non-trivial structural, functional and evolutionary information about proteins by iterative database searches
    • Aravind, L. and Koonin, E.V. 1999. Gleaning non-trivial structural, functional and evolutionary information about proteins by iterative database searches. J. Mol. Biol. 287: 1023-1040.
    • (1999) J. Mol. Biol , vol.287 , pp. 1023-1040
    • Aravind, L.1    Koonin, E.V.2
  • 3
    • 4444301974 scopus 로고    scopus 로고
    • Rational design of solution additives for the preventing of protein aggregation
    • Baynes, B.M. and Trout, B.L. 2004. Rational design of solution additives for the preventing of protein aggregation. Biophys. J. 87: 1631-1639.
    • (2004) Biophys. J , vol.87 , pp. 1631-1639
    • Baynes, B.M.1    Trout, B.L.2
  • 6
    • 0032537483 scopus 로고    scopus 로고
    • Biosynthesis of 2-aceto-2-hydroxy acids: Acetolactate synthases and acetohydroxyacid synthases
    • Chipman, D., Barak, Z., and Schloss, J.V. 1998. Biosynthesis of 2-aceto-2-hydroxy acids: Acetolactate synthases and acetohydroxyacid synthases. Biochim. Biophys. Acta 1385: 401-419.
    • (1998) Biochim. Biophys. Acta , vol.1385 , pp. 401-419
    • Chipman, D.1    Barak, Z.2    Schloss, J.V.3
  • 7
    • 24044548711 scopus 로고    scopus 로고
    • Characterization of acetohydroxyacid synthase from Mycobacterium tuberculosis and the indentification ot its new inhibitor from screening of a chemical library
    • Choi, K.-J., Yu, Y.G., Hahn, H.G., Choi, J.-D., and Yoon, M.-Y. 2005. Characterization of acetohydroxyacid synthase from Mycobacterium tuberculosis and the indentification ot its new inhibitor from screening of a chemical library. FEBS Lett. 579: 4903-4910.
    • (2005) FEBS Lett , vol.579 , pp. 4903-4910
    • Choi, K.-J.1    Yu, Y.G.2    Hahn, H.G.3    Choi, J.-D.4    Yoon, M.-Y.5
  • 8
    • 0002583957 scopus 로고
    • Joint CCP4 and ESF-EACBM newsletter
    • Cowtan, K. 1994. Joint CCP4 and ESF-EACBM newsletter. Protein Crystallogr. 31: 34-38.
    • (1994) Protein Crystallogr , vol.31 , pp. 34-38
    • Cowtan, K.1
  • 9
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. and Cowtan, K. 2004. Coot: Model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60: 2126-2132.
    • (2004) Acta Crystallogr. D Biol. Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 10
    • 0031718499 scopus 로고    scopus 로고
    • Inhibitors of branched-chain amino acid biosynthesis as potential antituberculosis agents
    • Grandoni, J.A., Marta, P.T., and Schloss, J.V. 1998. Inhibitors of branched-chain amino acid biosynthesis as potential antituberculosis agents. J. Antimicrob. Chemother. 42: 475-482.
    • (1998) J. Antimicrob. Chemother , vol.42 , pp. 475-482
    • Grandoni, J.A.1    Marta, P.T.2    Schloss, J.V.3
  • 12
    • 0036014793 scopus 로고    scopus 로고
    • Metal-ligand geometry relevant to proteins and in proteins: Sodium and potassium
    • Harding, M.M. 2002. Metal-ligand geometry relevant to proteins and in proteins: Sodium and potassium. Acta Crystallogr. D Biol. Crystallogr. 58: 872-874.
    • (2002) Acta Crystallogr. D Biol. Crystallogr , vol.58 , pp. 872-874
    • Harding, M.M.1
  • 13
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowan, S.W., and Kjeldgaard, M. 1991. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47: 110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 15
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure aligment in three dimensions
    • Krissinel, E. and Henrick, K. 2004. Secondary-structure matching (SSM), a new tool for fast protein structure aligment in three dimensions. Acta Crystallogr. D Biol. Crystallogr. 60: 2256-2268.
    • (2004) Acta Crystallogr. D Biol. Crystallogr , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 16
    • 0030596528 scopus 로고    scopus 로고
    • Crystal structure of bacterial lipase from Chromobacterium viscosum ATCC 6918 refined at 1.6Å resolution
    • Lang, D., Hofmann, B., Haalck, L., Hecht, H.-J., Spener, F., Schmid, R.D., and Schomburg, D. 1996. Crystal structure of bacterial lipase from Chromobacterium viscosum ATCC 6918 refined at 1.6Å resolution. J. Mol. Biol. 259: 704-717.
    • (1996) J. Mol. Biol , vol.259 , pp. 704-717
    • Lang, D.1    Hofmann, B.2    Haalck, L.3    Hecht, H.-J.4    Spener, F.5    Schmid, R.D.6    Schomburg, D.7
  • 17
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S., and Thornton, J.M. 1993. PROCHECK: A program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26: 283-291.
    • (1993) J. Appl. Crystallogr , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 18
    • 22544441094 scopus 로고    scopus 로고
    • ProFunc: A server for predicting protein function from 3D structure
    • Laskowski, R.A., Watson, J.D., and Thornton, J.M. 2005. ProFunc: A server for predicting protein function from 3D structure. Nucleic Acids Res. 33: W89-W93.
    • (2005) Nucleic Acids Res , vol.33
    • Laskowski, R.A.1    Watson, J.D.2    Thornton, J.M.3
  • 21
    • 0035949483 scopus 로고    scopus 로고
    • Structure of rat BCKD kinase: Nucleotide-induced domain communication in a mitochondrial protein kinase
    • Machius, M., Chuang, J.L., Wynn, R.M., Tomchick, D.R., and Chuang, D.T. 2001. Structure of rat BCKD kinase: Nucleotide-induced domain communication in a mitochondrial protein kinase. Proc. Natl. Acad. Sci. 98: 11218-11223.
    • (2001) Proc. Natl. Acad. Sci , vol.98 , pp. 11218-11223
    • Machius, M.1    Chuang, J.L.2    Wynn, R.M.3    Tomchick, D.R.4    Chuang, D.T.5
  • 22
    • 0035896041 scopus 로고    scopus 로고
    • Acetohydroxyacid synthase: A proposed structure for regulatory subunits supported by evidence from mutagenesis
    • Mendel, S., Elkayam, T., Sella, C., Vinogradov, V., Vyazmensky, M., Chipman, D.M., and Barak, Z. 2001. Acetohydroxyacid synthase: A proposed structure for regulatory subunits supported by evidence from mutagenesis. J. Mol. Biol. 307: 465-477.
    • (2001) J. Mol. Biol , vol.307 , pp. 465-477
    • Mendel, S.1    Elkayam, T.2    Sella, C.3    Vinogradov, V.4    Vyazmensky, M.5    Chipman, D.M.6    Barak, Z.7
  • 23
    • 0037229214 scopus 로고    scopus 로고
    • The N-terminal domain of the regulatory subunit is sufficient for complete activation of acetohydroxyacid synthase III from Escherichia coli
    • Mendel, S., Vinogradov, M., Vyazmensky, M., Chipman, D.M., and Barak, Z. 2003. The N-terminal domain of the regulatory subunit is sufficient for complete activation of acetohydroxyacid synthase III from Escherichia coli. J. Mol. Biol. 325: 275-284.
    • (2003) J. Mol. Biol , vol.325 , pp. 275-284
    • Mendel, S.1    Vinogradov, M.2    Vyazmensky, M.3    Chipman, D.M.4    Barak, Z.5
  • 24
    • 33745933955 scopus 로고    scopus 로고
    • HKL-3000: The integration of data reduction and structure solution - From diffraction images to an initial model in minutes
    • Minor, W., Cymborowski, M., Otwinowski, Z., and Chruszcz, M. 2006. HKL-3000: The integration of data reduction and structure solution - From diffraction images to an initial model in minutes. Acta Crystallogr. D Biol. Crystallogr. 62: 859-866.
    • (2006) Acta Crystallogr. D Biol. Crystallogr , vol.62 , pp. 859-866
    • Minor, W.1    Cymborowski, M.2    Otwinowski, Z.3    Chruszcz, M.4
  • 26
    • 0027435346 scopus 로고
    • The crystal structure of triacylglycerol lipase from Pseudomonas glumae reveals a partially redundant catalytic aspartate
    • Noble, M.E.M., Cleasby, A., Johnson, L.N., Egmond, M.R., and Frenken, L.G.L. 1993. The crystal structure of triacylglycerol lipase from Pseudomonas glumae reveals a partially redundant catalytic aspartate. FEBS Lett. 331: 123-128.
    • (1993) FEBS Lett , vol.331 , pp. 123-128
    • Noble, M.E.M.1    Cleasby, A.2    Johnson, L.N.3    Egmond, M.R.4    Frenken, L.G.L.5
  • 28
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • eds. Carter, C.W. Jr, and R.M. Sweet, Academic Press, New York
    • Otwinowski, Z. and Minor, W. 1997. Processing of X-ray diffraction data collected in oscillation mode. In Methods in enzymology: Macromolecular crystallography, part A. (eds. Carter, C.W. Jr., and R.M. Sweet). Vol. 276, pp. 307-326. Academic Press, New York.
    • (1997) Methods in enzymology: Macromolecular crystallography, part A , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 29
    • 33645158291 scopus 로고    scopus 로고
    • TLSMD web server for the generation of multi-group TLS models
    • Painter, J. and Merritt, E.A. 2006. TLSMD web server for the generation of multi-group TLS models. J. Appl. Crystallogr. 39: 109-111.
    • (2006) J. Appl. Crystallogr , vol.39 , pp. 109-111
    • Painter, J.1    Merritt, E.A.2
  • 30
    • 0000660166 scopus 로고    scopus 로고
    • Expression, purification, characterization, and reconstruction of the large and small subunits of yeast acetohydroxy-acid synthase
    • Pang, S.S. and Duggleby, R.G. 1999. Expression, purification, characterization, and reconstruction of the large and small subunits of yeast acetohydroxy-acid synthase. Biochemistry 38: 5222-5231.
    • (1999) Biochemistry , vol.38 , pp. 5222-5231
    • Pang, S.S.1    Duggleby, R.G.2
  • 31
    • 0029836483 scopus 로고    scopus 로고
    • Characterization of the metal ion binding helix-hairpin-helix motifs in human dna polymerase β by X-ray structural analysis
    • Pelletier, H. and Sawaya, M.R. 1996. Characterization of the metal ion binding helix-hairpin-helix motifs in human dna polymerase β by X-ray structural analysis. Biochemistry 35: 12778-12787.
    • (1996) Biochemistry , vol.35 , pp. 12778-12787
    • Pelletier, H.1    Sawaya, M.R.2
  • 33
    • 0141669302 scopus 로고    scopus 로고
    • Automatic inference of protein quaternary structure from crystals
    • Postingl, H., Kabir, T., and Thornton, J.M. 2003. Automatic inference of protein quaternary structure from crystals. J. Appl. Crystallogr. 36: 1116-1122.
    • (2003) J. Appl. Crystallogr , vol.36 , pp. 1116-1122
    • Postingl, H.1    Kabir, T.2    Thornton, J.M.3
  • 36
    • 33947503808 scopus 로고    scopus 로고
    • Institüt für Anorganische Chemie der Universität, Gottingen, Germany
    • Sheldrick, G.M. 1997. SHELXL-97 program for crystal structure refinement, vol. 4, p. D-3400. Institüt für Anorganische Chemie der Universität, Gottingen, Germany.
    • (1997) SHELXL-97 program for crystal structure refinement , vol.4
    • Sheldrick, G.M.1
  • 37
    • 0013054388 scopus 로고    scopus 로고
    • Macromolecular phasing with SHELXE
    • Sheldrick, G.M. 2002. Macromolecular phasing with SHELXE. Z. Kristallogr. 217: 644-650.
    • (2002) Z. Kristallogr , vol.217 , pp. 644-650
    • Sheldrick, G.M.1
  • 38
    • 0033363366 scopus 로고    scopus 로고
    • Pesticide use in the U.S. and policy implications: A focus on herbicides
    • Short, P. and Colborn, T. 1999. Pesticide use in the U.S. and policy implications: A focus on herbicides. Toxicol. Ind. Health 15: 240-275.
    • (1999) Toxicol. Ind. Health , vol.15 , pp. 240-275
    • Short, P.1    Colborn, T.2
  • 40
    • 0036848846 scopus 로고    scopus 로고
    • Automated structure solution, density modification and model building
    • Terwilliger, T.C. 2002. Automated structure solution, density modification and model building. Acta Crystallogr. D Biol. Crystallogr. 58: 1937-1940.
    • (2002) Acta Crystallogr. D Biol. Crystallogr , vol.58 , pp. 1937-1940
    • Terwilliger, T.C.1
  • 43
    • 0017794395 scopus 로고
    • Amino acid biosynthesis and its regulation
    • Umbarger, H.E. 1978. Amino acid biosynthesis and its regulation. Annu. Rev. Biochem. 47: 533-606.
    • (1978) Annu. Rev. Biochem , vol.47 , pp. 533-606
    • Umbarger, H.E.1
  • 44
    • 34250804453 scopus 로고    scopus 로고
    • Umbarger, H.E. 1987. Biosynthesis of branched chain aminoacids. In Escherichia coli and Salmonella typhimurium: Cellular and molecular biology (eds. F.C. Neidhardt et al.), pp. 352-367. American Society for Microbiology, Washington, DC.
    • Umbarger, H.E. 1987. Biosynthesis of branched chain aminoacids. In Escherichia coli and Salmonella typhimurium: Cellular and molecular biology (eds. F.C. Neidhardt et al.), pp. 352-367. American Society for Microbiology, Washington, DC.
  • 45
    • 0029798076 scopus 로고    scopus 로고
    • Isolation and characterization of subunits of acetohydroxy acid synthase isozyme III and reconstitution of the holoenzyme
    • Vyazmensky, M., Sella, C., Barak, Z., and Chipman, D.M. 1996. Isolation and characterization of subunits of acetohydroxy acid synthase isozyme III and reconstitution of the holoenzyme. Biochemistry 35: 10339-10346.
    • (1996) Biochemistry , vol.35 , pp. 10339-10346
    • Vyazmensky, M.1    Sella, C.2    Barak, Z.3    Chipman, D.M.4
  • 46
    • 0026804680 scopus 로고
    • Properties of subcloned subunits of bacterial acetohydroxy acid synthases
    • Weinstock, O., Sella, C., Chipman, D.M., and Barak, Z. 1992. Properties of subcloned subunits of bacterial acetohydroxy acid synthases. J. Bacteriol. 174: 5560-5566.
    • (1992) J. Bacteriol , vol.174 , pp. 5560-5566
    • Weinstock, O.1    Sella, C.2    Chipman, D.M.3    Barak, Z.4
  • 48
    • 0043123259 scopus 로고    scopus 로고
    • Acetohydroxyacid synthase from Mycobacterium avium and its inhibition by sulfonylureas and imidazolinones
    • Zohar, Y., Einav, M., Chipman, D.M., and Barak, Z. 2003. Acetohydroxyacid synthase from Mycobacterium avium and its inhibition by sulfonylureas and imidazolinones. Biochim. Biophys. Acta 1649: 97-105.
    • (2003) Biochim. Biophys. Acta , vol.1649 , pp. 97-105
    • Zohar, Y.1    Einav, M.2    Chipman, D.M.3    Barak, Z.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.