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7n7z
From Proteopedia
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==Structure of Acetyl-CoA acetyltransferase from Syntrophomonas wolfei== | ==Structure of Acetyl-CoA acetyltransferase from Syntrophomonas wolfei== | ||
| - | <StructureSection load='7n7z' size='340' side='right'caption='[[7n7z]]' scene=''> | + | <StructureSection load='7n7z' size='340' side='right'caption='[[7n7z]], [[Resolution|resolution]] 2.02Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7N7Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7N7Z FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7n7z]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Syntrophomonas_wolfei_subsp._wolfei_str._Goettingen_G311 Syntrophomonas wolfei subsp. wolfei str. Goettingen G311]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7N7Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7N7Z FirstGlance]. <br> |
</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=7n7z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7n7z OCA], [https://pdbe.org/7n7z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7n7z RCSB], [https://www.ebi.ac.uk/pdbsum/7n7z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7n7z ProSAT]</span></td></tr> | </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=7n7z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7n7z OCA], [https://pdbe.org/7n7z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7n7z RCSB], [https://www.ebi.ac.uk/pdbsum/7n7z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7n7z ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q0AZ52_SYNWW Q0AZ52_SYNWW] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Syntrophomonas wolfei is an anaerobic syntrophic microbe that degrades short-chain fatty acids to acetate, hydrogen, and/or formate. This thermodynamically unfavorable process proceeds through a series of reactive acyl-Coenzyme A species (RACS). In other prokaryotic and eukaryotic systems, the production of intrinsically reactive metabolites correlates with acyl-lysine modifications, which have been shown to play a significant role in metabolic processes. Analogous studies with syntrophic bacteria, however, are relatively unexplored and we hypothesized that highly abundant acylations could exist in S. wolfei proteins, corresponding to the RACS derived from degrading fatty acids. Here, by mass spectrometry-based proteomics (LC-MS/MS), we characterize and compare acylome profiles of two S. wolfei subspecies grown on different carbon substrates. Because modified S. wolfei proteins are sufficiently abundant to analyze post-translational modifications (PTMs) without antibody enrichment, we could identify types of acylations comprehensively, observing six types (acetyl-, butyryl-, 3-hydroxybutyryl-, crotonyl-, valeryl-, and hexanyl-lysine), two of which have not been reported in any system previously. All of the acyl-PTMs identified correspond directly to RACS in fatty acid degradation pathways. A total of 369 sites of modification were identified on 237 proteins. Structural studies and in vitro acylation assays of a heavily modified enzyme, acetyl-CoA transferase, provided insight on the potential impact of these acyl-protein modifications. The extensive changes in acylation-type, abundance, and modification sites with carbon substrate suggest that protein acylation by RACS may be an important regulator of syntrophy. | ||
| + | |||
| + | Dynamic acylome reveals metabolite driven modifications in Syntrophomonas wolfei.,Fu JY, Muroski JM, Arbing MA, Salguero JA, Wofford NQ, McInerney MJ, Gunsalus RP, Loo JA, Ogorzalek Loo RR Front Microbiol. 2022 Nov 7;13:1018220. doi: 10.3389/fmicb.2022.1018220. , eCollection 2022. PMID:36419437<ref>PMID:36419437</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7n7z" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| + | [[Category: Syntrophomonas wolfei subsp. wolfei str. Goettingen G311]] | ||
[[Category: Arbing MA]] | [[Category: Arbing MA]] | ||
[[Category: Gunsalus RP]] | [[Category: Gunsalus RP]] | ||
Revision as of 07:45, 11 January 2023
Structure of Acetyl-CoA acetyltransferase from Syntrophomonas wolfei
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