1zfn

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|PDB= 1zfn |SIZE=350|CAPTION= <scene name='initialview01'>1zfn</scene>, resolution 2.75&Aring;
|PDB= 1zfn |SIZE=350|CAPTION= <scene name='initialview01'>1zfn</scene>, resolution 2.75&Aring;
|SITE=
|SITE=
-
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=ATP:ADENOSINE-5&#39;-TRIPHOSPHATE'>ATP</scene>
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|LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5&#39;-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
|ACTIVITY=
|ACTIVITY=
|GENE= thiF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
|GENE= thiF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
 +
|DOMAIN=
 +
|RELATEDENTRY=[[1jwa|1JWA]], [[1jw9|1JW9]], [[1jwb|1JWB]]
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zfn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zfn OCA], [http://www.ebi.ac.uk/pdbsum/1zfn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zfn RCSB]</span>
}}
}}
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[[Category: Sfondouris, J.]]
[[Category: Sfondouris, J.]]
[[Category: Walden, H.]]
[[Category: Walden, H.]]
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[[Category: ATP]]
 
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[[Category: ZN]]
 
[[Category: adenylation]]
[[Category: adenylation]]
[[Category: atp-binding]]
[[Category: atp-binding]]
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[[Category: these]]
[[Category: these]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 14:28:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:35:21 2008''

Revision as of 22:35, 30 March 2008

Image:1zfn.gif


PDB ID 1zfn

Drag the structure with the mouse to rotate
, resolution 2.75Å
Ligands: ,
Gene: thiF (Escherichia coli)
Related: 1JWA, 1JW9, 1JWB


Resources: FirstGlance, OCA, PDBsum, RCSB
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

1ZFN 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

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