6cul: Difference between revisions
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<StructureSection load='6cul' size='340' side='right'caption='[[6cul]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='6cul' size='340' side='right'caption='[[6cul]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6cul]] is a 8 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6cul]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseae Pseae]. 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 [https://proteopedia.org/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> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pvdF, PA2396 ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pvdF, PA2396 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=208964 PSEAE])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6cul FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cul OCA], [https://pdbe.org/6cul PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cul RCSB], [https://www.ebi.ac.uk/pdbsum/6cul PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cul ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
Revision as of 13:16, 18 March 2021
PvdF of pyoverdin biosynthesis is a structurally unique N10-formyltetrahydrofolate-dependent formyltransferasePvdF of pyoverdin biosynthesis is a structurally unique N10-formyltetrahydrofolate-dependent formyltransferase
Structural highlights
Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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