6cul: Difference between revisions

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-'''Unreleased structure'''
-The entry 6cul is ON HOLD  until Paper Publication
+==PvdF of pyoverdin biosynthesis is a structurally unique N10-formyltetrahydrofolate-dependent formyltransferase==
+<StructureSection load='6cul' size='340' side='right' caption='[[6cul]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6cul]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CUL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CUL FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=FGD:N-(4-{[(2-amino-4-oxo-1,4-dihydroquinazolin-6-yl)methyl]amino}benzene-1-carbonyl)-D-glutamic+acid'>FGD</scene></td></tr>
+<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=6cul FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cul OCA], [http://pdbe.org/6cul PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cul RCSB], [http://www.ebi.ac.uk/pdbsum/6cul PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cul ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The hydroxyornithine transformylase from Pseudomonas aeruginosa is known by the gene name pvdF, and has been hypothesized to use N(10)-formyltetrahydrofolate (N(10)-fTHF) as a co-substrate formyl donor to convert N(5)-hydroxyornithine (OHOrn) to N(5)-formyl- N(5)-hydroxyornithine (fOHOrn). PvdF is in the biosynthetic pathway for pyoverdin biosynthesis, a siderophore generated under iron-limiting conditions that has been linked to virulence, quorum sensing and biofilm formation. The structure of PvdF was determined by X-ray crystallography to 2.3A, revealing a formyltransferase fold consistent with N(10)-formyltetrahydrofolate dependent enzymes, such as the glycinamide ribonucleotide transformylases, N-sugar transformylases and methionyl-tRNA transformylases. Whereas the core structure, including the catalytic triad, is conserved, PvdF has three insertions of 18 or more amino acids, which we hypothesize are key to binding the OHOrn substrate. Steady state kinetics revealed a non-hyperbolic rate curve, promoting the hypothesis that PvdF uses a random-sequential mechanism, and favors folate binding over OHOrn.
-Authors:
+PvdF of pyoverdin biosynthesis is a structurally unique N(10)-formyltetrahydrofolate-dependent formyltransferase.,Kenjic N, Hoag MR, Moraski GC, Caperelli CA, Moran GR, Lamb AL Arch Biochem Biophys. 2019 Jan 26;664:40-50. doi: 10.1016/j.abb.2019.01.028. PMID:30689984<ref>PMID:30689984</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6cul" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Caperelli, C A]]
+[[Category: Hoag, M R]]
+[[Category: Kenjic, N]]
+[[Category: Lamb, A L]]
+[[Category: Moran, G R]]
+[[Category: Moraski, G C]]
+[[Category: N10-formyltetrahydrofolate-dependent formyltransferase]]
+[[Category: Transferase]]