6cul: Difference between revisions
New page: '''Unreleased structure''' The entry 6cul is ON HOLD Authors: Description: Category: Unreleased Structures |
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The | ==PvdF of pyoverdin biosynthesis is a structurally unique N10-formyltetrahydrofolate-dependent formyltransferase== | ||
<StructureSection load='6cul' size='340' side='right'caption='[[6cul]], [[Resolution|resolution]] 2.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6cul]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</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>, <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'>[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> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9I184_PSEAE Q9I184_PSEAE] | |||
<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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6cul" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pseudomonas aeruginosa PAO1]] | |||
[[Category: Caperelli CA]] | |||
[[Category: Hoag MR]] | |||
[[Category: Kenjic N]] | |||
[[Category: Lamb AL]] | |||
[[Category: Moran GR]] | |||
[[Category: Moraski GC]] | |||
Latest revision as of 08:08, 21 November 2024
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
FunctionPublication 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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