Structural analysis of Escherichia coli ThiF - PubMed (original) (raw)
Structural analysis of Escherichia coli ThiF
David M Duda et al. J Mol Biol. 2005.
Abstract
Escherichia coli ThiF is an enzyme in the biosynthetic cascade for generating the essential cofactor thiamin pyrophosphate. In this cascade, ThiF catalyzes adenylation of the C terminus of ThiS. We report here the crystal structures of ThiF, alone and in complex with ATP. The structures provide insight into a preference for ATP during adenylation of the protein ThiS. Additionally, the structures reveal an ordered crossover loop predicted to clamp the flexible tail of ThiS into the ThiF active site during the adenylation reaction. The importance of the crossover loop for ThiF activity is highlighted by mutational analysis. Comparison of ThiF with the structural homologues MoeB, APPBP1-UBA3, and SAE1-SAE2 reveals that the ATP-binding site, including an arginine-finger, is maintained throughout evolution, and shows divergence occurring in protein substrate-binding sites and regions devoted to unique steps in the specific function of each enzyme.
Similar articles
- Structure of the Escherichia coli ThiS-ThiF complex, a key component of the sulfur transfer system in thiamin biosynthesis.
Lehmann C, Begley TP, Ealick SE. Lehmann C, et al. Biochemistry. 2006 Jan 10;45(1):11-9. doi: 10.1021/bi051502y. Biochemistry. 2006. PMID: 16388576 Free PMC article. - Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex.
Lake MW, Wuebbens MM, Rajagopalan KV, Schindelin H. Lake MW, et al. Nature. 2001 Nov 15;414(6861):325-9. doi: 10.1038/35104586. Nature. 2001. PMID: 11713534 - Closing the gap on DNA ligase.
Shuman S. Shuman S. Structure. 1996 Jun 15;4(6):653-6. doi: 10.1016/s0969-2126(96)00070-6. Structure. 1996. PMID: 8805556 Review.
Cited by
- Common thiolation mechanism in the biosynthesis of tRNA thiouridine and sulphur-containing cofactors.
Shigi N, Sakaguchi Y, Asai S, Suzuki T, Watanabe K. Shigi N, et al. EMBO J. 2008 Dec 17;27(24):3267-78. doi: 10.1038/emboj.2008.246. Epub 2008 Nov 27. EMBO J. 2008. PMID: 19037260 Free PMC article. - Clostridiolysin S, a post-translationally modified biotoxin from Clostridium botulinum.
Gonzalez DJ, Lee SW, Hensler ME, Markley AL, Dahesh S, Mitchell DA, Bandeira N, Nizet V, Dixon JE, Dorrestein PC. Gonzalez DJ, et al. J Biol Chem. 2010 Sep 3;285(36):28220-8. doi: 10.1074/jbc.M110.118554. Epub 2010 Jun 25. J Biol Chem. 2010. PMID: 20581111 Free PMC article. - Origin and function of ubiquitin-like proteins.
Hochstrasser M. Hochstrasser M. Nature. 2009 Mar 26;458(7237):422-9. doi: 10.1038/nature07958. Nature. 2009. PMID: 19325621 Free PMC article. Review. - Biosynthesis of Thiamin Pyrophosphate.
Jurgenson CT, Ealick SE, Begley TP. Jurgenson CT, et al. EcoSal Plus. 2009 Aug;3(2):10.1128/ecosalplus.3.6.3.7. doi: 10.1128/ecosalplus.3.6.3.7. EcoSal Plus. 2009. PMID: 26443755 Free PMC article. - Crystal structure of the human ubiquitin-activating enzyme 5 (UBA5) bound to ATP: mechanistic insights into a minimalistic E1 enzyme.
Bacik JP, Walker JR, Ali M, Schimmer AD, Dhe-Paganon S. Bacik JP, et al. J Biol Chem. 2010 Jun 25;285(26):20273-80. doi: 10.1074/jbc.M110.102921. Epub 2010 Apr 5. J Biol Chem. 2010. PMID: 20368332 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Molecular Biology Databases