4avc

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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]] 2.81&Aring;' scene=''>
<StructureSection load='4avc' size='340' side='right' caption='[[4avc]], [[Resolution|resolution]] 2.81&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4avc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AVC FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4avc]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AVC FirstGlance]. <br>
</td></tr><tr id='ligand'><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>
</td></tr><tr id='ligand'><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='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='related'><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">[[4ava|4ava]], [[4avb|4avb]]</td></tr>
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<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=4avc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4avc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4avc RCSB], [http://www.ebi.ac.uk/pdbsum/4avc PDBsum]</span></td></tr>
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<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=4avc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4avc OCA], [http://pdbe.org/4avc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4avc RCSB], [http://www.ebi.ac.uk/pdbsum/4avc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4avc ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/O05581_MYCTU O05581_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>
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[[http://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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 4avc" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Mycobacterium tuberculosis]]
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[[Category: Myctu]]
[[Category: Alber, T]]
[[Category: Alber, T]]
[[Category: Fortune, S M]]
[[Category: Fortune, S M]]

Revision as of 18:44, 4 August 2016

Crystal structure of protein lysine acetyltransferase Rv0998 in complex with acetyl CoA and cAMP

4avc, resolution 2.81Å

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