3n6r

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[[Image:3n6r.png|left|200px]]
 
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==CRYSTAL STRUCTURE OF the holoenzyme of PROPIONYL-COA CARBOXYLASE (PCC)==
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The line below this paragraph, containing "STRUCTURE_3n6r", creates the "Structure Box" on the page.
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<StructureSection load='3n6r' size='340' side='right'caption='[[3n6r]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3n6r]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Roseobacter_denitrificans_OCh_114 Roseobacter denitrificans OCh 114] and [https://en.wikipedia.org/wiki/Ruegeria_pomeroyi Ruegeria pomeroyi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3N6R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3N6R FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 3.2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BTI:5-(HEXAHYDRO-2-OXO-1H-THIENO[3,4-D]IMIDAZOL-6-YL)PENTANAL'>BTI</scene></td></tr>
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{{STRUCTURE_3n6r| PDB=3n6r | SCENE= }}
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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=3n6r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n6r OCA], [https://pdbe.org/3n6r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3n6r RCSB], [https://www.ebi.ac.uk/pdbsum/3n6r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3n6r ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PCCA_RUEPO PCCA_RUEPO] This is one of the 2 subunits of the biotin-dependent propionyl-CoA carboxylase (PCC), the enzyme catalyzing the carboxylation of propionyl-CoA/propanoyl-CoA to D-methylmalonyl-CoA/(S)-methylmalonyl-CoA (PubMed:20725044). Within the holoenzyme, the alpha subunit catalyzes the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain, while the beta subunit then tranfers the carboxyl group from carboxylated biotin to propionyl-CoA (Probable).<ref>PMID:20725044</ref> <ref>PMID:20725044</ref>
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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/n6/3n6r_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=3n6r ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Propionyl-coenzyme A carboxylase (PCC), a mitochondrial biotin-dependent enzyme, is essential for the catabolism of the amino acids Thr, Val, Ile and Met, cholesterol and fatty acids with an odd number of carbon atoms. Deficiencies in PCC activity in humans are linked to the disease propionic acidaemia, an autosomal recessive disorder that can be fatal in infants. The holoenzyme of PCC is an alpha(6)beta(6) dodecamer, with a molecular mass of 750 kDa. The alpha-subunit contains the biotin carboxylase (BC) and biotin carboxyl carrier protein (BCCP) domains, whereas the beta-subunit supplies the carboxyltransferase (CT) activity. Here we report the crystal structure at 3.2-A resolution of a bacterial PCC alpha(6)beta(6) holoenzyme as well as cryo-electron microscopy (cryo-EM) reconstruction at 15-A resolution demonstrating a similar structure for human PCC. The structure defines the overall architecture of PCC and reveals unexpectedly that the alpha-subunits are arranged as monomers in the holoenzyme, decorating a central beta(6) hexamer. A hitherto unrecognized domain in the alpha-subunit, formed by residues between the BC and BCCP domains, is crucial for interactions with the beta-subunit. We have named it the BT domain. The structure reveals for the first time the relative positions of the BC and CT active sites in the holoenzyme. They are separated by approximately 55 A, indicating that the entire BCCP domain must translocate during catalysis. The BCCP domain is located in the active site of the beta-subunit in the current structure, providing insight for its involvement in the CT reaction. The structural information establishes a molecular basis for understanding the large collection of disease-causing mutations in PCC and is relevant for the holoenzymes of other biotin-dependent carboxylases, including 3-methylcrotonyl-CoA carboxylase (MCC) and eukaryotic acetyl-CoA carboxylase (ACC).
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===CRYSTAL STRUCTURE OF the holoenzyme of PROPIONYL-COA CARBOXYLASE (PCC)===
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Crystal structure of the alpha(6)beta(6) holoenzyme of propionyl-coenzyme A carboxylase.,Huang CS, Sadre-Bazzaz K, Shen Y, Deng B, Zhou ZH, Tong L Nature. 2010 Aug 19;466(7309):1001-5. PMID:20725044<ref>PMID:20725044</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_20725044}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3n6r" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 20725044 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_20725044}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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[[3n6r]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Roseobacter_denitrificans_och_114 Roseobacter denitrificans och 114] and [http://en.wikipedia.org/wiki/Ruegeria_pomeroyi Ruegeria pomeroyi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3N6R OCA].
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[[Category: Roseobacter denitrificans OCh 114]]
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==Reference==
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<ref group="xtra">PMID:20725044</ref><references group="xtra"/>
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[[Category: Propionyl-CoA carboxylase]]
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[[Category: Roseobacter denitrificans och 114]]
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[[Category: Ruegeria pomeroyi]]
[[Category: Ruegeria pomeroyi]]
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[[Category: Huang, C S.]]
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[[Category: Huang CS]]
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[[Category: Sadre-Bazzaz, K.]]
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[[Category: Sadre-Bazzaz K]]
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[[Category: Tong, L.]]
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[[Category: Tong L]]

Current revision

CRYSTAL STRUCTURE OF the holoenzyme of PROPIONYL-COA CARBOXYLASE (PCC)

PDB ID 3n6r

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