Crystal structure of methenyltetrahydrofolate synthetase from Mycoplasma pneumoniae (GI: 13508087) at 2.2 Å resolution

Proteins: Structure, Function and Genetics

Volumn 56, Issue 4, 2004, Pages 839-843

  Chen, Shengfeng ^a,b   Shin, Dong Hae ^b   Pufan, Ramona ^b   Kim, Rosalind ^b   Kim, Sung Hou ^a,b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b LAWRENCE BERKELEY NATIONAL LABORATORY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; GLUTACONATE COENZYME A TRANSFERASE; METHYLENETETRAHYDROFOLATE SYNTHETASE; METHYLENETETRAHYDROFOLIC ACID; RPIA PROTEIN; SYNTHETASE; TRANSFERASE; UNCLASSIFIED DRUG;

ARTICLE; CRYSTAL STRUCTURE; CRYSTALLIZATION; ENZYME ACTIVE SITE; ENZYME STRUCTURE; MYCOPLASMA PNEUMONIAE; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PURIFICATION; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; X RAY DIFFRACTION;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BINDING SITES; CARBON-NITROGEN LIGASES; CLONING, MOLECULAR; CRYSTALLOGRAPHY, X-RAY; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; MYCOPLASMA PNEUMONIAE; PEPTIDE MAPPING; SEQUENCE HOMOLOGY, AMINO ACID;

BACTERIA (MICROORGANISMS); MYCOPLASMA; MYCOPLASMA PNEUMONIAE;

EID: 4043166166     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20214     Document Type: Article

References (25)

1. Belanger C, MacKenzie RE. Structural organization of the murine gene encoding NAD-dependent methylenetetrahydrofolate dehydrogenase- methenyltetrahydrofolate cyclohydrolase. Gene 1991;97:283-288.
2. Kan JL, Jannatipour M, Taylor SM, Moran RG. Mouse cDNAs encoding a trifunctional protein of de novo purine synthesis and a related single-domain glycinamide ribonucleotide synthetase. Gene 1993;137:195-202.
3. Shane B. Folylpolyglutamate synthesis and role in the regulation of one-carbon metabolism. Vitam Horm 1989;45:263-335.
4. Wagner C. In Bailey LB, editor. Folate in Health and Disease, New York: Marcel Dekker, Inc; 1995, p 23-42, chapter 2, Biochemical Role of Folate in Cellular Metabolism.
5. Selhub J. Homocysteine metabolism. Annu Rev Nutr 1999;19: 217-246.
6. Shane B. In Bailey LB, editor. Folate in Health and Disease, New York: Marcel Dekker, Inc; 1995, p 1-22, chapter 1, Folate Chemistry and Metabolism.
7. Clarke S, Banfield K. In Carmel R, Jacobson DW, editor. Homocysteine in Health and Disease, Cambridge: Cambridge Press; 2001. p 63-78, chapter 7, S-adenosylmethionine-dependent methyltransferases.
8. Kim R, Sandler SJ, Goldman S, Yokota H, Clark AJ, Kim S-H. Overexpression of archaeal proteins in Escherichia coli. Biotechnol. Lett 1998;20:207-210.
9. Doublie, S. Preparation of selenomethionyl proteins for phase determination. Methods Enzymol 1997;276:523-529.
10. Jancarik J, Kim S-H. Sparse matrix sampling: A screening method for crystallization of proteins. J Appl Crystallogr 1991;24: 409-411.
11. Otwinowski Z, Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 1996;276:307-326.
12. Terwilliger T, Berendzen J. Automated MAD and MIR structure solution. Acta Crystallogr. D 1999;55:849-861.
13. Cowtan K. Joint CCP4 and ESF-EACBM Newsletter on Protein Crystallography. 1994;31:34-38.
14. Brünger AT, Adams PD, Clore GM, Delano WL, Gros P, Grosse-Kunstleve RW, Jiang JS, Kuszewski J, Nilges M, Pannu NS. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallog. D 1998;54:905-921.
15. Jones, TA, Zou, J-Y, Cowan, SW, Kjeldgaard, M. Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 1991;47: 110-119.
16. Kraulis P. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 1991;24: 946-950.
17. Nicholls A, Sharp KA, Honig B. Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 1991;11:281-296.
18. Altschul SF, Gish W, Miller W, Myers EW, Lipman DJ. Basic local alignment search tool. J Mol Biol 1990;215:403-410.
19. Luzzati V. Traitement statistique des erreurs dans la determinationn des structures cristallines. Acta Crystallogr 1952;5:802-810.
20. Laskowski RA, MacArthur MW, Moss DS, Thornton JM. PROCHECK: A program to check the stereochemical quality of protein structures. J Appl Crystallog 1993;26:283-291.
21. Holm L, Sander C. Mapping the protein universe. Science 1996;273: 595-603.
22. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE. The Protein Data Bank. Nucleic Acids Res 2000;28:235-242.
23. Rangarajan ES, Sivaraman J, Matte A, Cygler M. Crystal structure of D-ribose-5-phosphate isomerase (RpiA) from Escherichia coli. Proteins 2002;48:737-740.
24. Zhang R, Andersson CE, Savchenko A, Skarina T, Evdokimova E, Beasley S, Arrowsmith CH, Edwards AM, Joachimiak A, Mowbray SL. Structure of Escherichia coli ribose-5-phosphate isomerase: a ubiquitous enzyme of the pentose phosphate pathway and the Calvin cycle. Structure Fold Des 2003;11:31-42.
25. Jacob U, Mack M, Clausen T, Huber R, Buckel W, Messerschmidt A. Glutaconate CoA-transferase from Acidaminococcus fermentans: the crystal structure reveals homology with other CoA-transferases. Structure Fold Des 1997;5:415-426.