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| | ==cAMP-binding acyltransferase from Mycobacterium smegmatis== | | ==cAMP-binding acyltransferase from Mycobacterium smegmatis== |
| - | <StructureSection load='4oll' size='340' side='right' caption='[[4oll]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='4oll' size='340' side='right'caption='[[4oll]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4oll]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycs2 Mycs2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OLL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OLL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4oll]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis_MC2_155 Mycolicibacterium smegmatis MC2 155]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OLL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OLL FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4oll FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oll OCA], [https://pdbe.org/4oll PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4oll RCSB], [https://www.ebi.ac.uk/pdbsum/4oll PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4oll ProSAT]</span></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4onu|4onu]], [[4orf|4orf]]</td></tr>
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| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MSMEG_5458, MSMEI_5308 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=246196 MYCS2])</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=4oll FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oll OCA], [http://pdbe.org/4oll PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4oll RCSB], [http://www.ebi.ac.uk/pdbsum/4oll PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4oll ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PAT_MYCS2 PAT_MYCS2]] Catalyzes specifically the acetylation of the epsilon-amino group of a highly conserved lysine residue in acetyl-CoA synthetase (ACS) and of the universal stress protein (USP) MSMEG_4207. 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> | + | [https://www.uniprot.org/uniprot/PAT_MYCS2 PAT_MYCS2] Catalyzes specifically the acetylation of the epsilon-amino group of a highly conserved lysine residue in acetyl-CoA synthetase (ACS) and of the universal stress protein (USP) MSMEG_4207. 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> |
| | <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: Mycs2]] | + | [[Category: Large Structures]] |
| - | [[Category: Podobnik, M]] | + | [[Category: Mycolicibacterium smegmatis MC2 155]] |
| - | [[Category: Rebolj, K]] | + | [[Category: Podobnik M]] |
| - | [[Category: Visweswariah, S S]] | + | [[Category: Rebolj K]] |
| - | [[Category: Acyl-transferase domain]] | + | [[Category: Visweswariah SS]] |
| - | [[Category: Alpha-beta fold]]
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| - | [[Category: Apo-enzyme]]
| + | |
| - | [[Category: Cyclic nucleotide binding domain]]
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| - | [[Category: Linker peptide]]
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| - | [[Category: Transferase]]
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| Structural highlights
Function
PAT_MYCS2 Catalyzes specifically the acetylation of the epsilon-amino group of a highly conserved lysine residue in acetyl-CoA synthetase (ACS) and of the universal stress protein (USP) MSMEG_4207. Acetylation results in the inactivation of ACS activity and could be important for mycobacteria to adjust to environmental changes.[1] [2]
Publication Abstract from PubMed
Mycobacteria harbor unique proteins that regulate protein lysine acylation in a cAMP-regulated manner. These lysine acyltransferases from Mycobacterium smegmatis (KATms) and Mycobacterium tuberculosis (KATmt) show distinctive biochemical properties in terms of cAMP binding affinity to the N-terminal cyclic nucleotide binding domain and allosteric activation of the C-terminal acyltransferase domain. Here we provide evidence for structural features in KATms that account for high affinity cAMP binding and elevated acyltransferase activity in the absence of cAMP. Structure-guided mutational analysis converted KATms from a cAMP-regulated to a cAMP-dependent acyltransferase and identified a unique asparagine residue in the acyltransferase domain of KATms that assists in the enzymatic reaction in the absence of a highly conserved glutamate residue seen in Gcn5-related N-acetyltransferase-like acyltransferases. Thus, we have identified mechanisms by which properties of similar proteins have diverged in two species of mycobacteria by modifications in amino acid sequence, which can dramatically alter the abundance of conformational states adopted by a protein.
Allostery and Conformational Dynamics in cAMP-binding Acyltransferases.,Podobnik M, Siddiqui N, Rebolj K, Nambi S, Merzel F, Visweswariah SS J Biol Chem. 2014 Jun 6;289(23):16588-16600. Epub 2014 Apr 18. PMID:24748621[3]
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
- ↑ Podobnik M, Siddiqui N, Rebolj K, Nambi S, Merzel F, Visweswariah SS. Allostery and Conformational Dynamics in cAMP-binding Acyltransferases. J Biol Chem. 2014 Jun 6;289(23):16588-16600. Epub 2014 Apr 18. PMID:24748621 doi:http://dx.doi.org/10.1074/jbc.M114.560086
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