4avc: Difference between revisions
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==Crystal structure of protein lysine acetyltransferase Rv0998 in complex with acetyl CoA and cAMP== | ==Crystal structure of protein lysine acetyltransferase Rv0998 in complex with acetyl CoA and cAMP== | ||
<StructureSection load='4avc' size='340' side='right' caption='[[4avc]], [[Resolution|resolution]] 2.81Å' scene=''> | <StructureSection load='4avc' size='340' side='right'caption='[[4avc]], [[Resolution|resolution]] 2.81Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4avc]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4avc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AVC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AVC FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=CMP:ADENOSINE-3,5-CYCLIC-MONOPHOSPHATE'>CMP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=CMP:ADENOSINE-3,5-CYCLIC-MONOPHOSPHATE'>CMP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> | ||
<tr><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><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ava|4ava]], [[4avb|4avb]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4ava|4ava]], [[4avb|4avb]]</div></td></tr> | ||
<tr><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=4avc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4avc OCA], [https://pdbe.org/4avc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4avc RCSB], [https://www.ebi.ac.uk/pdbsum/4avc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4avc ProSAT]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[https://www.uniprot.org/uniprot/PAT_MYCTU PAT_MYCTU]] Catalyzes specifically the acetylation of the epsilon-amino group of a highly conserved lysine residue in acetyl-CoA synthetase (ACS). This acetylation results in the inactivation of ACS activity and could be important for mycobacteria to adjust to environmental changes.<ref>PMID:20507997</ref> <ref>PMID:21627103</ref> <ref>PMID:22773105</ref> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4avc" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Alber, T | [[Category: Myctu]] | ||
[[Category: Fortune, S M | [[Category: Alber, T]] | ||
[[Category: Lang, P T | [[Category: Fortune, S M]] | ||
[[Category: Lee, H J | [[Category: Lang, P T]] | ||
[[Category: Sassetti, C M | [[Category: Lee, H J]] | ||
[[Category: Sassetti, C M]] | |||
[[Category: Acetyltransferase]] | [[Category: Acetyltransferase]] | ||
[[Category: Allosteric regulation]] | [[Category: Allosteric regulation]] | ||
[[Category: Domain coupling]] | [[Category: Domain coupling]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||