7wx6: Difference between revisions
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==A Legionella acetyltransferase VipF== | |||
<StructureSection load='7wx6' size='340' side='right'caption='[[7wx6]], [[Resolution|resolution]] 2.27Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7wx6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Legionella_pneumophila Legionella pneumophila]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=7c4g 7c4g]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7WX6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WX6 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CLM:CHLORAMPHENICOL'>CLM</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</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=7wx6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wx6 OCA], [https://pdbe.org/7wx6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wx6 RCSB], [https://www.ebi.ac.uk/pdbsum/7wx6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wx6 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[https://www.uniprot.org/uniprot/Q5C8M4_LEGPN Q5C8M4_LEGPN]] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The pathogen Legionella pneumophila, which is the causative agent of Legionnaires' disease, secrets hundreds of effectors into host cells via its Dot/Icm secretion system to subvert host-cell pathways during pathogenesis. VipF, a conserved core effector among Legionella species, is a putative acetyltransferase, but its structure and catalytic mechanism remain unknown. Here, three crystal structures of VipF in complex with its cofactor acetyl-CoA and/or a substrate are reported. The two GNAT-like domains of VipF are connected as two wings by two beta-strands to form a U-shape. Both domains bind acetyl-CoA or CoA, but only in the C-terminal domain does the molecule extend to the bottom of the U-shaped groove as required for an active transferase reaction; the molecule in the N-terminal domain folds back on itself. Interestingly, when chloramphenicol, a putative substrate, binds in the pocket of the central U-shaped groove adjacent to the N-terminal domain, VipF remains in an open conformation. Moreover, mutations in the central U-shaped groove, including Glu129 and Asp251, largely impaired the acetyltransferase activity of VipF, suggesting a unique enzymatic mechanism for the Legionella effector VipF. | |||
Structural basis for the acetylation mechanism of the Legionella effector VipF.,Chen TT, Lin Y, Zhang S, Han A Acta Crystallogr D Struct Biol. 2022 Sep 1;78(Pt 9):1110-1119. doi:, 10.1107/S2059798322007318. Epub 2022 Aug 9. PMID:36048151<ref>PMID:36048151</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 7wx6" style="background-color:#fffaf0;"></div> | ||
[[Category: Chen | == References == | ||
[[Category: Chen | <references/> | ||
[[Category: Lin | __TOC__ | ||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Legionella pneumophila]] | |||
[[Category: Chen TT]] | |||
[[Category: Chen Z]] | |||
[[Category: Han AD]] | |||
[[Category: Lin YL]] | |||
Revision as of 06:51, 14 September 2022
A Legionella acetyltransferase VipF
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