View source for 4yfv


==X-ray structure of the 4-N-formyltransferase VioF from Providencia alcalifaciens O30==
<StructureSection load='4yfv' size='340' side='right'caption='[[4yfv]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4yfv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Providencia_alcalifaciens Providencia alcalifaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YFV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YFV FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.89&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4yfv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yfv OCA], [https://pdbe.org/4yfv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yfv RCSB], [https://www.ebi.ac.uk/pdbsum/4yfv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yfv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/M9P0Q2_9GAMM M9P0Q2_9GAMM] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The existence of N-formylated sugars in the O-antigens of Gram-negative bacteria has been known since the middle 1980s, but only recently have the biosynthetic pathways for their production been reported. In these pathways, glucose-1-phosphate is first activated by attachment to a dTMP moiety. This step is followed by a dehydration reaction and an amination. The last step in these pathways is catalyzed by N-formyltransferases that utilize N10 -formyltetrahydrofolate as the carbon source. Here we describe the three-dimensional structure of one of these N-formyltransferases, namely VioF from Providencia alcalifaciens O30. Specifically, this enzyme catalyzes the conversion of dTDP-4-amino-6-deoxyglucose (dTDP-Qui4N) to dTDP-4,6-dideoxy-4-formamido-d-glucose (dTDP-Qui4NFo). For this analysis, the structure of VioF was solved to 1.9 A resolution in both its apoform and in complex with tetrahydrofolate and dTDP-Qui4N. The crystals used in the investigation belonged to the space group R32 and demonstrated reticular merohedral twinning. The overall catalytic core of the VioF subunit is characterized by a six stranded mixed beta-sheet flanked on one side by three alpha-helices and on the other side by mostly random coil. This N-terminal domain is followed by an alpha-helix and a beta-hairpin that form the subunit:subunit interface. The active site of the enzyme is shallow and solvent-exposed. Notably, the pyranosyl moiety of dTDP-Qui4N is positioned into the active site by only one hydrogen bond provided by Lys 77. Comparison of the VioF model to that of a previously determined N-formyltransferase suggests that substrate specificity is determined by interactions between the protein and the pyrophosphoryl group of the dTDP-sugar substrate. This article is protected by copyright. All rights reserved.

Molecular Structure of an N-formyltransferase from Providencia alcalifaciens O30.,Genthe NA, Thoden JB, Benning MM, Holden HM Protein Sci. 2015 Mar 9. doi: 10.1002/pro.2675. PMID:25752909<ref>PMID:25752909</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4yfv" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Providencia alcalifaciens]]
[[Category: Benning MM]]
[[Category: Genthe NA]]
[[Category: Holden HM]]
[[Category: Thoden JB]]