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| | <StructureSection load='4avb' size='340' side='right'caption='[[4avb]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='4avb' size='340' side='right'caption='[[4avb]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4avb]] 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=4AVB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AVB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4avb]] 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=4AVB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AVB 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=ACT:ACETATE+ION'>ACT</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" id="ligandDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ava|4ava]], [[4avc|4avc]]</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]], [[4avc|4avc]]</div></td></tr> |
| - | <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=4avb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4avb OCA], [http://pdbe.org/4avb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4avb RCSB], [http://www.ebi.ac.uk/pdbsum/4avb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4avb ProSAT]</span></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=4avb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4avb OCA], [https://pdbe.org/4avb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4avb RCSB], [https://www.ebi.ac.uk/pdbsum/4avb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4avb ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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> | + | [[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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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | [[Category: Myctu]] | | [[Category: Myctu]] |
| | [[Category: Alber, T]] | | [[Category: Alber, T]] |
| Structural highlights
Function
[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.[1] [2] [3]
Publication Abstract from PubMed
Protein lysine acetylation networks can regulate central processes such as carbon metabolism and gene expression in bacteria. In Escherichia coli, cyclic AMP (cAMP) regulates protein lysine acetyltransferase (PAT) activity at the transcriptional level, but in Mycobacterium tuberculosis, fusion of a cyclic nucleotide-binding domain to a Gcn5-like PAT domain enables direct cAMP control of protein acetylation. Here we describe the allosteric activation mechanism of M. tuberculosis PAT. The crystal structures of the autoinhibited and cAMP-activated PAT reveal that cAMP binds to a cryptic site in the regulatory domain that is over 32 A from the catalytic site. An extensive conformational rearrangement relieves this autoinhibition by means of a substrate-mimicking lid that covers the protein-substrate binding surface. A steric double latch couples the domains by harnessing a classic, cAMP-mediated conformational switch. The structures suggest general features that enable the evolution of long-range communication between linked domains.
Cyclic AMP regulation of protein lysine acetylation in Mycobacterium tuberculosis.,Lee HJ, Lang PT, Fortune SM, Sassetti CM, Alber T Nat Struct Mol Biol. 2012 Aug 3;19(8):811-8. doi: 10.1038/nsmb.2318. Epub 2012, Jul 8. PMID:22773105[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nambi S, Basu N, Visweswariah SS. cAMP-regulated protein lysine acetylases in mycobacteria. J Biol Chem. 2010 Aug 6;285(32):24313-23. doi: 10.1074/jbc.M110.118398. Epub 2010, May 27. PMID:20507997 doi:http://dx.doi.org/10.1074/jbc.M110.118398
- ↑ Xu H, Hegde SS, Blanchard JS. Reversible acetylation and inactivation of Mycobacterium tuberculosis acetyl-CoA synthetase is dependent on cAMP. Biochemistry. 2011 Jul 5;50(26):5883-92. doi: 10.1021/bi200156t. Epub 2011 Jun, 10. PMID:21627103 doi:http://dx.doi.org/10.1021/bi200156t
- ↑ Lee HJ, Lang PT, Fortune SM, Sassetti CM, Alber T. Cyclic AMP regulation of protein lysine acetylation in Mycobacterium tuberculosis. Nat Struct Mol Biol. 2012 Aug 3;19(8):811-8. doi: 10.1038/nsmb.2318. Epub 2012, Jul 8. PMID:22773105 doi:10.1038/nsmb.2318
- ↑ Lee HJ, Lang PT, Fortune SM, Sassetti CM, Alber T. Cyclic AMP regulation of protein lysine acetylation in Mycobacterium tuberculosis. Nat Struct Mol Biol. 2012 Aug 3;19(8):811-8. doi: 10.1038/nsmb.2318. Epub 2012, Jul 8. PMID:22773105 doi:10.1038/nsmb.2318
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