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| | ==Structural studies on the interaction of ScFAS ACP with ACPS== | | ==Structural studies on the interaction of ScFAS ACP with ACPS== |
| - | <StructureSection load='2cnr' size='340' side='right' caption='[[2cnr]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2cnr' size='340' side='right'caption='[[2cnr]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2cnr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Strco Strco]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CNR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CNR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2cnr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor_A3(2) Streptomyces coelicolor A3(2)]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CNR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CNR FirstGlance]. <br> |
| - | </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=2cnr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cnr OCA], [http://pdbe.org/2cnr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cnr RCSB], [http://www.ebi.ac.uk/pdbsum/2cnr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2cnr ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2cnr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cnr OCA], [https://pdbe.org/2cnr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cnr RCSB], [https://www.ebi.ac.uk/pdbsum/2cnr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cnr ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/P72393_STRCH P72393_STRCH]] Carrier of the growing fatty acid chain in fatty acid biosynthesis.[HAMAP-Rule:MF_01217][RuleBase:RU003545] | + | [https://www.uniprot.org/uniprot/P72393_STRCH P72393_STRCH] Carrier of the growing fatty acid chain in fatty acid biosynthesis.[HAMAP-Rule:MF_01217][RuleBase:RU003545] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Acyl carrier protein|Acyl carrier protein]] | + | *[[Acyl carrier protein 3D structures|Acyl carrier protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Strco]] | + | [[Category: Large Structures]] |
| - | [[Category: Crump, M P]] | + | [[Category: Crump MP]] |
| - | [[Category: Pottage, K]] | + | [[Category: Pottage K]] |
| - | [[Category: Williams, C]] | + | [[Category: Williams C]] |
| - | [[Category: Acp]]
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| - | [[Category: Fa]]
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| - | [[Category: Lipid transport]]
| + | |
| - | [[Category: Phosphopantetheine]]
| + | |
| - | [[Category: Polykdetide]]
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| Structural highlights
Function
P72393_STRCH Carrier of the growing fatty acid chain in fatty acid biosynthesis.[HAMAP-Rule:MF_01217][RuleBase:RU003545]
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 PubMed
Malonylation of an acyl carrier protein (ACP) by malonyl Coenzyme A-ACP transacylase (MCAT) is fundamental to bacterial fatty acid biosynthesis. Here, we report the structure of the Steptomyces coelicolor (Sc) fatty acid synthase (FAS) ACP and studies of its binding to MCAT. The carrier protein adopts an alpha-helical bundle structure common to other known carrier proteins. The Sc FAS ACP shows close structural homology with other fatty acid ACPs and less similarity with Sc actinorhodin (act) polyketide synthase (PKS) ACP where the orientation of helix I differs. NMR experiments were used to map the binding of ACP to MCAT. This data suggests that Sc FAS ACP interacts with MCAT through the negatively charged helix II of ACP, consistent with proposed models for ACP recognition by other FAS enzymes. Differential roles for residues at the interface are demonstrated using site-directed mutagenesis and in vitro assays. MCAT has been suggested, moreover, to participate in bacterial polyketide synthesis in vivo. We demonstrate that the affinity of the polyketide synthase ACP for MCAT is lower than that of the FAS ACP. Mutagenesis of homologous helix II residues on the polyketide synthase ACP suggests that the PKS ACP may bind to MCAT in a different manner than the FAS counterpart.
Structure and malonyl CoA-ACP transacylase binding of streptomyces coelicolor fatty acid synthase acyl carrier protein.,Arthur CJ, Williams C, Pottage K, Ploskon E, Findlow SC, Burston SG, Simpson TJ, Crump MP, Crosby J ACS Chem Biol. 2009 Aug 21;4(8):625-36. PMID:19555075[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Arthur CJ, Williams C, Pottage K, Ploskon E, Findlow SC, Burston SG, Simpson TJ, Crump MP, Crosby J. Structure and malonyl CoA-ACP transacylase binding of streptomyces coelicolor fatty acid synthase acyl carrier protein. ACS Chem Biol. 2009 Aug 21;4(8):625-36. PMID:19555075 doi:10.1021/cb900099e
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