Crystal structures of a phosphotransacetylase from Bacillus subtilis and its complex with acetyl phosphate

Journal of Structural and Functional Genomics

Volumn 6, Issue 4, 2005, Pages 269-279

  Qian, Steven Xu ^a   Jancarik, Jarmila ^b   Lou, Yun ^a   Kuznetsova, Kate ^c   Yakunin, Alexander F ^c   Yokota, Hisao ^a   Adams, Paul ^a   Kim, Rosalind ^a   Kim, Sung Hou ^a,b  

^a LAWRENCE BERKELEY NATIONAL LABORATORY   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c UNIVERSITY OF TORONTO   (Canada)

Author keywords

Bacillus subtilis; Berkeley Structural Genomics Center (BSGC); Crystal structure; GI16080818; Phosphotransacetylase; Structural genomics

Indexed keywords

4 HYDROXYTHREONINE 4 PHOSPHATE DEHYDROGENASE; ACETIC ACID; ACETIC ACID DERIVATIVE; ACETYL PHOSPHATE; BACTERIAL ENZYME; COENZYME A; ISOCITRATE DEHYDROGENASE; ISOPROPYLMALATE DEHYDROGENASE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; OXIDOREDUCTASE; PHOSPHATE; PHOSPHATE ACETYLTRANSFERASE; UNCLASSIFIED DRUG;

ARTICLE; BACILLUS SUBTILIS; BINDING SITE; COMPLEX FORMATION; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME LOCALIZATION; ENZYME MECHANISM; ENZYME SUBSTRATE COMPLEX; METABOLISM; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING;

AMINO ACID SEQUENCE; BACILLUS SUBTILIS; BINDING SITES; COENZYME A; CRYSTALLOGRAPHY, X-RAY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PHOSPHATE ACETYLTRANSFERASE; PHOSPHORIC ACID ESTERS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID; STRUCTURAL HOMOLOGY, PROTEIN;

BACILLUS SUBTILIS; BACTERIA (MICROORGANISMS);

EID: 33646467387     PISSN: 1345711X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10969-005-9001-9     Document Type: Article

References (20)

1. Henkin, J. and Abeles, R.H. (1976) Biochemistry 15, 3472-3479.
2. Iyer, P.P. and Ferry, J.G. (2001) J. Bacteriol. 183, 4244-4250.
3. Rasche, M.E., Smith, K.S. and Ferry, J.G. (1997) J. Bacteriol. 179, 7712-7717.
4. Iyer, P.P., Lawrence, S.H., Luther, K.B., Rajashankar, K.R., Yennawar, H.P., Ferry, J.G. and Schindelin, H. (2004) Structure 12, 559-567.
5. Xu, Q.S., Shin, D.-H., Pufan, R., Yokota, H., Kim, R. and Kim, S.-H. (2004) Proteins Struct. Funct. Bioinformat. 55, 479-481.
6. Rado, T.A. and Hoch, J.A. (1973) Biochim. Biophys. Acta 321, 114-125.
7. Kim, R., Sandler, S.J., Goldman, S., Yokota, H., Clark, A.J. and Kim, S.-H. (1998) Biotechnol. Letts. 20, 207-210.
8. Jancarik, J. and Kim, S.-H. (1991) J. Appl. Crystallogr. 24, 409-411.
9. Otwinowski, Z. and Minor, W. (1997) Methods Enzymol. 276, 307-326.
10. Brunger, A.T., Adams, P.D., Clore, G.M., DeLano, W.L., Gros, P., Grosse-Kunstleve, R.W., Jiang, J.S., Kuszewski, J., Nilges, M., Pannu, N.S., Read, R.J., Rice, L.M., Simonson, T. and Warren, G.L. (1998) Acta Crystallogr. D. Biol. Crystallogr. 54, 905-921.
11. Jones, T.A., Zou, J.Y., Cowan, S.W. and Murshudov, G.N., Vagin, A.A. and Dodson, E.J. (1997) Acta Crystallogr. D Biol. Crystallogr. 53, 240-255.
12. Kleywegt, G.J. and Jones, T.A. (1998) Acta Crystallogr. D Biol. Crystallogr. 54, 1119-1131.
13. Whiteley, H.R. and Pelroy, R.A. (1972) J. Biol. Chem. 247, 1911-1917.
14. Rossmann, M.G., Moras, D. and Olsen, K.W. (1974) Nature 250, 194-199.
15. Holm, L. and Sander, C. (1996) Science 273, 595-603.
16. Sivaraman, J., Li, Y., Banks, J., Cane, D.E., Matte, A. and Cygler, M. (2003) J. Biol. Chem. 278, 43682-43690.
17. Lundie, L.L. Jr and Ferry, J.G. (1989) J. Biol. Chem. 264, 18392-18396.
18. Bock, A.K., Glasemacher, J., Schmidt, R. and Schönheit, P. (1999) J. Bacteriol. 181, 1861-1867.
19. Kraulis, P.J. (1991) J. Appl. Crystallogr. 24, 946-950.
20. Merritt, E.A. (1994) Acta Crystallogr. D Biol. Crystallogr. 50, 869-873.