2f9i: Difference between revisions
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==Crystal Structure of the carboxyltransferase subunit of ACC from Staphylococcus aureus== | ==Crystal Structure of the carboxyltransferase subunit of ACC from Staphylococcus aureus== | ||
<StructureSection load='2f9i' size='340' side='right' caption='[[2f9i]], [[Resolution|resolution]] 1.98Å' scene=''> | <StructureSection load='2f9i' size='340' side='right' caption='[[2f9i]], [[Resolution|resolution]] 1.98Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2f9y|2f9y]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2f9y|2f9y]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACCA,ACCD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 "Micrococcus aureus" (Rosenbach 1884) Zopf 1885])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACCA,ACCD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 "Micrococcus aureus" (Rosenbach 1884) Zopf 1885])</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=2f9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f9i OCA], [http://pdbe.org/2f9i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2f9i RCSB], [http://www.ebi.ac.uk/pdbsum/2f9i PDBsum]</span></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=2f9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f9i OCA], [http://pdbe.org/2f9i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2f9i RCSB], [http://www.ebi.ac.uk/pdbsum/2f9i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2f9i ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2f9i ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</div> | </div> | ||
<div class="pdbe-citations 2f9i" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2f9i" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 10:35, 18 October 2017
Crystal Structure of the carboxyltransferase subunit of ACC from Staphylococcus aureusCrystal Structure of the carboxyltransferase subunit of ACC from Staphylococcus aureus
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedAcetyl-coA carboxylase (ACC) is a central metabolic enzyme that catalyzes the committed step in fatty acid biosynthesis: biotin-dependent conversion of acetyl-coA to malonyl-coA. The bacterial carboxyltransferase (CT) subunit of ACC is a target for the design of novel therapeutics that combat severe, hospital-acquired infections resistant to the established classes of frontline antimicrobials. Here, we present the structures of the bacterial CT subunits from two prevalent nosocomial pathogens, Staphylococcus aureus and Escherichia coli, at a resolution of 2.0 and 3.0 A, respectively. Both structures reveal a small, independent zinc-binding domain that lacks a complement in the primary sequence or structure of the eukaryotic homologue. The structure of the carboxyltransferase component of acetyl-coA carboxylase reveals a zinc-binding motif unique to the bacterial enzyme.,Bilder P, Lightle S, Bainbridge G, Ohren J, Finzel B, Sun F, Holley S, Al-Kassim L, Spessard C, Melnick M, Newcomer M, Waldrop GL Biochemistry. 2006 Feb 14;45(6):1712-22. PMID:16460018[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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