1zfn

<StructureSection load='1zfn' size='340' side='right' caption='[[1zfn]], [[Resolution|resolution]] 2.75&Aring;' scene=''>

<table><tr><td colspan='2'>[[1zfn]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZFN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZFN FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jwa|1jwa]], [[1jw9|1jw9]], [[1jwb|1jwb]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">thiF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1zfn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zfn RCSB], [http://www.ebi.ac.uk/pdbsum/1zfn PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/THIF_ECOLI THIF_ECOLI]] Catalyzes the adenylation by ATP of the carboxyl group of the C-terminal glycine of sulfur carrier protein ThiS.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zf/1zfn_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:15896804</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1zfn" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Bacillus coli migula 1895]]

[[Category: Duda, D M]]

[[Category: Schulman, B A]]

[[Category: Sfondouris, J]]

[[Category: Walden, H]]

[[Category: Adenylation]]

[[Category: Transferase]]