1xnv

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[[Image:1xnv.jpg|left|200px]]<br /><applet load="1xnv" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1xnv, resolution 2.30&Aring;" />
 
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'''Acyl-CoA Carboxylase Beta Subunit from S. coelicolor (PccB), apo form #1'''<br />
 
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==Overview==
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==Acyl-CoA Carboxylase Beta Subunit from S. coelicolor (PccB), apo form #1==
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Acetyl-CoA carboxylase (ACC) and propionyl-CoA carboxylase (PCC) catalyze the carboxylation of acetyl- and propionyl-CoA to generate malonyl- and methylmalonyl-CoA, respectively. Understanding the substrate specificity of ACC and PCC will (1) help in the development of novel structure-based inhibitors that are potential therapeutics against obesity, cancer, and infectious disease and (2) facilitate bioengineering to provide novel extender units for polyketide biosynthesis. ACC and PCC in Streptomyces coelicolor are multisubunit complexes. The core catalytic beta-subunits, PccB and AccB, are 360 kDa homohexamers, catalyzing the transcarboxylation between biotin and acyl-CoAs. Apo and substrate-bound crystal structures of PccB hexamers were determined to 2.0-2.8 A. The hexamer assembly forms a ring-shaped complex. The hydrophobic, highly conserved biotin-binding pocket was identified for the first time. Biotin and propionyl-CoA bind perpendicular to each other in the active site, where two oxyanion holes were identified. N1 of biotin is proposed to be the active site base. Structure-based mutagenesis at a single residue of PccB and AccB allowed interconversion of the substrate specificity of ACC and PCC. The di-domain, dimeric interaction is crucial for enzyme catalysis, stability, and substrate specificity; these features are also highly conserved among biotin-dependent carboxyltransferases. Our findings enable bioengineering of the acyl-CoA carboxylase (ACCase) substrate specificity to provide novel extender units for the combinatorial biosynthesis of polyketides.
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<StructureSection load='1xnv' size='340' side='right'caption='[[1xnv]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1xnv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XNV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XNV FirstGlance]. <br>
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1XNV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Active as [http://en.wikipedia.org/wiki/Propionyl-CoA_carboxylase Propionyl-CoA carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.4.1.3 6.4.1.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XNV OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xnv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xnv OCA], [https://pdbe.org/1xnv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xnv RCSB], [https://www.ebi.ac.uk/pdbsum/1xnv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xnv ProSAT]</span></td></tr>
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==Reference==
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</table>
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Crystal structure of the beta-subunit of acyl-CoA carboxylase: structure-based engineering of substrate specificity., Diacovich L, Mitchell DL, Pham H, Gago G, Melgar MM, Khosla C, Gramajo H, Tsai SC, Biochemistry. 2004 Nov 9;43(44):14027-36. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15518551 15518551]
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== Function ==
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[[Category: Propionyl-CoA carboxylase]]
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[https://www.uniprot.org/uniprot/Q9X4K7_STRCH Q9X4K7_STRCH]
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[[Category: Single protein]]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xn/1xnv_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1xnv ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Streptomyces coelicolor]]
[[Category: Streptomyces coelicolor]]
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[[Category: Diacovich, L.]]
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[[Category: Diacovich L]]
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[[Category: Gago, G.]]
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[[Category: Gago G]]
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[[Category: Gramajo, H.]]
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[[Category: Gramajo H]]
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[[Category: Khosla, C.]]
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[[Category: Khosla C]]
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[[Category: Melgar, M M.]]
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[[Category: Melgar MM]]
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[[Category: Mitchell, D L.]]
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[[Category: Mitchell DL]]
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[[Category: Pham, H.]]
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[[Category: Pham H]]
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[[Category: Tsai, S C.]]
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[[Category: Tsai S-C]]
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[[Category: polyketide; polyketide synthase; acyl-coa carboxylase; carboxyltransferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:56:49 2008''
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Current revision

Acyl-CoA Carboxylase Beta Subunit from S. coelicolor (PccB), apo form #1

PDB ID 1xnv

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OCA

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