1zkm
From Proteopedia
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- | [[Image:1zkm.gif|left|200px]] | + | [[Image:1zkm.gif|left|200px]] |
- | + | ||
- | '''Structural Analysis of Escherichia Coli ThiF''' | + | {{Structure |
+ | |PDB= 1zkm |SIZE=350|CAPTION= <scene name='initialview01'>1zkm</scene>, resolution 2.95Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= thiF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
+ | }} | ||
+ | |||
+ | '''Structural Analysis of Escherichia Coli ThiF''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1ZKM is a [ | + | 1ZKM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZKM OCA]. |
==Reference== | ==Reference== | ||
- | Structural analysis of Escherichia coli ThiF., Duda DM, Walden H, Sfondouris J, Schulman BA, J Mol Biol. 2005 Jun 17;349(4):774-86. PMID:[http:// | + | Structural analysis of Escherichia coli ThiF., Duda DM, Walden H, Sfondouris J, Schulman BA, J Mol Biol. 2005 Jun 17;349(4):774-86. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15896804 15896804] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: rossman fold]] | [[Category: rossman fold]] | ||
[[Category: thif]] | [[Category: thif]] | ||
- | [[Category: | + | [[Category: these]] |
[[Category: ubiquitin]] | [[Category: ubiquitin]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:36:40 2008'' |
Revision as of 13:36, 20 March 2008
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, resolution 2.95Å | |||||||
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Ligands: | |||||||
Gene: | thiF (Escherichia coli) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Structural Analysis of Escherichia Coli ThiF
Overview
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.
About this Structure
1ZKM is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structural analysis of Escherichia coli ThiF., Duda DM, Walden H, Sfondouris J, Schulman BA, J Mol Biol. 2005 Jun 17;349(4):774-86. PMID:15896804
Page seeded by OCA on Thu Mar 20 15:36:40 2008
Categories: Escherichia coli | Single protein | Duda, D M. | Schulman, B A. | Sfondouris, J. | Walden, H. | ZN | Atp binding | Moeb | P-loop | Rossman fold | Thif | These | Ubiquitin