1zfn

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[[Image:1zfn.gif|left|200px]]
[[Image:1zfn.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1zfn |SIZE=350|CAPTION= <scene name='initialview01'>1zfn</scene>, resolution 2.75&Aring;
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The line below this paragraph, containing "STRUCTURE_1zfn", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5&#39;-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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or leave the SCENE parameter empty for the default display.
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|GENE= thiF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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-->
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|DOMAIN=
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{{STRUCTURE_1zfn| PDB=1zfn | SCENE= }}
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|RELATEDENTRY=[[1jwa|1JWA]], [[1jw9|1JW9]], [[1jwb|1JWB]]
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|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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}}
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'''Structural Analysis of Escherichia coli ThiF'''
'''Structural Analysis of Escherichia coli ThiF'''
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[[Category: Sfondouris, J.]]
[[Category: Sfondouris, J.]]
[[Category: Walden, H.]]
[[Category: Walden, H.]]
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[[Category: adenylation]]
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[[Category: Adenylation]]
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[[Category: atp-binding]]
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[[Category: Atp-binding]]
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[[Category: p-loop]]
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[[Category: P-loop]]
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[[Category: rossman fold]]
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[[Category: Rossman fold]]
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[[Category: thif]]
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[[Category: Thif]]
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[[Category: these]]
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[[Category: These]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:34:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:35:21 2008''
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Revision as of 14:34, 3 May 2008

Image:1zfn.gif

Template:STRUCTURE 1zfn

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 Page seeded by OCA on Sat May 3 17:34:03 2008

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