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1xnw

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[[Image:1xnw.jpg|left|200px]]
 
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{{Structure
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==Acyl-CoA Carboxylase Beta Subunit from S. coelicolor (PccB), apo form #2, mutant D422I==
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|PDB= 1xnw |SIZE=350|CAPTION= <scene name='initialview01'>1xnw</scene>, resolution 2.60&Aring;
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<StructureSection load='1xnw' size='340' side='right'caption='[[1xnw]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1xnw]] is a 6 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=1XNW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XNW FirstGlance]. <br>
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|ACTIVITY= [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]
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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]] 2.6&#8491;</td></tr>
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|GENE=
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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=1xnw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xnw OCA], [https://pdbe.org/1xnw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xnw RCSB], [https://www.ebi.ac.uk/pdbsum/1xnw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xnw ProSAT]</span></td></tr>
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}}
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</table>
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== Function ==
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'''Acyl-CoA Carboxylase Beta Subunit from S. coelicolor (PccB), apo form #2, mutant D422I'''
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[https://www.uniprot.org/uniprot/Q9X4K7_STRCH Q9X4K7_STRCH]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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==Overview==
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Check<jmol>
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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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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xn/1xnw_consurf.spt"</scriptWhenChecked>
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==About this Structure==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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1XNW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XNW OCA].
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==Reference==
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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=1xnw ConSurf].
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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://www.ncbi.nlm.nih.gov/pubmed/15518551 15518551]
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<div style="clear:both"></div>
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[[Category: Propionyl-CoA carboxylase]]
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__TOC__
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[[Category: Single protein]]
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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 Mar 20 15:12:21 2008''
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Current revision

Acyl-CoA Carboxylase Beta Subunit from S. coelicolor (PccB), apo form #2, mutant D422I

PDB ID 1xnw

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