1xny

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[[Image:1xny.jpg|left|200px]]
 
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{{Structure
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==Biotin and propionyl-CoA bound to Acyl-CoA Carboxylase Beta Subunit from S. coelicolor (PccB)==
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|PDB= 1xny |SIZE=350|CAPTION= <scene name='initialview01'>1xny</scene>, resolution 2.20&Aring;
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<StructureSection load='1xny' size='340' side='right'caption='[[1xny]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=191:PROPIONYL+COENZYME+A'>191</scene>, <scene name='pdbligand=BTN:BIOTIN'>BTN</scene>
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<table><tr><td colspan='2'>[[1xny]] 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=1XNY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XNY FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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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]] 2.2&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1VU:PROPIONYL+COENZYME+A'>1VU</scene>, <scene name='pdbligand=BTN:BIOTIN'>BTN</scene></td></tr>
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|DOMAIN=
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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=1xny FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xny OCA], [https://pdbe.org/1xny PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xny RCSB], [https://www.ebi.ac.uk/pdbsum/1xny PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xny ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1xnv|1XNV]], [[1xnw|1XNW]], [[1xo6|1XO6]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xny FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xny OCA], [http://www.ebi.ac.uk/pdbsum/1xny PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xny RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/Q9X4K7_STRCH Q9X4K7_STRCH]
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== Evolutionary Conservation ==
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'''Biotin and propionyl-CoA bound to Acyl-CoA Carboxylase Beta Subunit from S. coelicolor (PccB)'''
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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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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xn/1xny_consurf.spt"</scriptWhenChecked>
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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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<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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==About this Structure==
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</jmolCheckbox>
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1XNY 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=1XNY OCA].
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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=1xny ConSurf].
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<div style="clear:both"></div>
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==Reference==
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__TOC__
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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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</StructureSection>
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[[Category: Propionyl-CoA carboxylase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[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: acyl-coa carboxylase]]
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[[Category: carboxyltransferase]]
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[[Category: polyketide]]
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[[Category: polyketide synthase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:52:14 2008''
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Current revision

Biotin and propionyl-CoA bound to Acyl-CoA Carboxylase Beta Subunit from S. coelicolor (PccB)

PDB ID 1xny

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