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| | ==Structure of ATP bound RpMatB-BxBclM chimera B3== | | ==Structure of ATP bound RpMatB-BxBclM chimera B3== |
| - | <StructureSection load='4gxr' size='340' side='right' caption='[[4gxr]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='4gxr' size='340' side='right'caption='[[4gxr]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4gxr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhopa Rhopa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GXR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GXR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4gxr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Paraburkholderia_xenovorans_LB400 Paraburkholderia xenovorans LB400] and [https://en.wikipedia.org/wiki/Rhodopseudomonas_palustris_CGA009 Rhodopseudomonas palustris CGA009]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GXR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GXR FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</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=4gxr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gxr OCA], [https://pdbe.org/4gxr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gxr RCSB], [https://www.ebi.ac.uk/pdbsum/4gxr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gxr ProSAT]</span></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4fut|4fut]], [[4fuq|4fuq]], [[2v7b|2v7b]], [[4gxq|4gxq]], [[3nyr|3nyr]], [[3nyq|3nyq]]</td></tr>
| + | |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">matB, RPA0221 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=258594 RHOPA])</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=4gxr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gxr OCA], [http://pdbe.org/4gxr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4gxr RCSB], [http://www.ebi.ac.uk/pdbsum/4gxr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4gxr ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q13WK3_PARXL Q13WK3_PARXL] [https://www.uniprot.org/uniprot/Q6ND88_RHOPA Q6ND88_RHOPA] |
| | <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: Rhopa]] | + | [[Category: Large Structures]] |
| - | [[Category: Crosby, H A]] | + | [[Category: Paraburkholderia xenovorans LB400]] |
| - | [[Category: Escalante-Semerena, J C]] | + | [[Category: Rhodopseudomonas palustris CGA009]] |
| - | [[Category: Rank, K C]] | + | [[Category: Crosby HA]] |
| - | [[Category: Rayment, I]] | + | [[Category: Escalante-Semerena JC]] |
| - | [[Category: Acetylation of k488 by rppat]]
| + | [[Category: Rank KC]] |
| - | [[Category: Anl-superfamily]]
| + | [[Category: Rayment I]] |
| - | [[Category: Coa]] | + | |
| - | [[Category: Ligase]] | + | |
| - | [[Category: Malonate]]
| + | |
| - | [[Category: Malonate-coa ligase]]
| + | |
| - | [[Category: Methylmalonate]]
| + | |
| - | [[Category: Methylmalonate-coa ligase]]
| + | |
| - | [[Category: Rpmatb-bxbclm chimera]]
| + | |
| Structural highlights
4gxr is a 1 chain structure with sequence from Paraburkholderia xenovorans LB400 and Rhodopseudomonas palustris CGA009. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
Q13WK3_PARXL Q6ND88_RHOPA
Publication Abstract from PubMed
Lysine acetylation is a post-translational modification that is important for the regulation of metabolism in both prokaryotes and eukaryotes. In bacteria, the best studied protein acetyltransferase is Pat. In the purple photosynthetic bacterium Rhodopseudomonas palustris, at least 10 AMP-forming acyl-CoA synthetase enzymes are acetylated by the Pat homologue RpPat. All bona fide RpPat substrates contain the conserved motif PX(4)GK. Here, we show that the presence of such a motif is necessary but not sufficient for recognition by RpPat. RpPat failed to acetylate the methylmalonyl-CoA synthetase of this bacterium (hereafter RpMatB) in vivo and in vitro, despite the homology of RpMatB to known RpPat substrates. We used RpMatB to identify structural determinants that are recognized by RpPat. To do this, we constructed a series of RpMatB chimeras that became substrates of RpPat. In such chimeras, a short region (11-25 residues) of RpMatB located >20 residues N-terminal to the acetylation site was replaced with the corresponding sequences from other AMP-forming acyl-CoA synthetases that were known RpPat substrates. Strikingly, the enzymatic activity of RpMatB chimeras was regulated by acetylation both in vitro and in vivo. Crystal structures of two of these chimeras showed that the major difference between them and wild-type RpMatB was within a loop region approximately 23 A from the acetylation site. On the basis of these results, we suggest that RpPat likely interacts with a relatively large surface of its substrates, in addition to the PX(4)GK motif, and that RpPat probably has relatively narrow substrate specificity.
Structural Insights into the Substrate Specificity of the Rhodopseudomonas palustris Protein Acetyltransferase RpPat: IDENTIFICATION OF A LOOP CRITICAL FOR RECOGNITION BY RpPat.,Crosby HA, Rank KC, Rayment I, Escalante-Semerena JC J Biol Chem. 2012 Nov 30;287(49):41392-404. doi: 10.1074/jbc.M112.417360. Epub, 2012 Oct 17. PMID:23076154[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Crosby HA, Rank KC, Rayment I, Escalante-Semerena JC. Structural Insights into the Substrate Specificity of the Rhodopseudomonas palustris Protein Acetyltransferase RpPat: IDENTIFICATION OF A LOOP CRITICAL FOR RECOGNITION BY RpPat. J Biol Chem. 2012 Nov 30;287(49):41392-404. doi: 10.1074/jbc.M112.417360. Epub, 2012 Oct 17. PMID:23076154 doi:http://dx.doi.org/10.1074/jbc.M112.417360
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