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5h80

From Proteopedia

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'''Unreleased structure'''
 
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The entry 5h80 is ON HOLD
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==Biotin Carboxylase domain of single-chain bacterial carboxylase==
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<StructureSection load='5h80' size='340' side='right'caption='[[5h80]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5h80]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H80 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5H80 FirstGlance]. <br>
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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]] 1.7&#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=EDO:1,2-ETHANEDIOL'>EDO</scene></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=5h80 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h80 OCA], [https://pdbe.org/5h80 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5h80 RCSB], [https://www.ebi.ac.uk/pdbsum/5h80 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5h80 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q9RYK2_DEIRA Q9RYK2_DEIRA]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Biotin-dependent acyl-coenzyme A (CoA) carboxylases (aCCs) are involved in key steps of anabolic pathways and comprise three distinct functional units: biotin carboxylase (BC), biotin carboxyl carrier protein (BCCP), and carboxyl transferase (CT). YCC multienzymes are a poorly characterized family of prokaryotic aCCs of unidentified substrate specificity, which integrate all functional units into a single polypeptide chain. We employed a hybrid approach to study the dynamic structure of Deinococcus radiodurans (Dra) YCC: crystal structures of isolated domains reveal a hexameric CT core with extended substrate binding pocket and a dimeric BC domain. Negative-stain electron microscopy provides an approximation of the variable positioning of the BC dimers relative to the CT core. Small-angle X-ray scattering yields quantitative information on the ensemble of Dra YCC structures in solution. Comparison with other carrier protein-dependent multienzymes highlights a characteristic range of large-scale interdomain flexibility in this important class of biosynthetic enzymes.
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Authors: Hagmann, A., Hunkeler, M., Stuttfeld, E., Maier, T.
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Hybrid Structure of a Dynamic Single-Chain Carboxylase from Deinococcus radiodurans.,Hagmann A, Hunkeler M, Stuttfeld E, Maier T Structure. 2016 Jul 6. pii: S0969-2126(16)30120-4. doi:, 10.1016/j.str.2016.06.001. PMID:27396827<ref>PMID:27396827</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Stuttfeld, E]]
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<div class="pdbe-citations 5h80" style="background-color:#fffaf0;"></div>
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[[Category: Hunkeler, M]]
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== References ==
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[[Category: Maier, T]]
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<references/>
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[[Category: Hagmann, A]]
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__TOC__
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</StructureSection>
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[[Category: Deinococcus radiodurans]]
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[[Category: Large Structures]]
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[[Category: Hagmann A]]
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[[Category: Hunkeler M]]
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[[Category: Maier T]]
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[[Category: Stuttfeld E]]

Current revision

Biotin Carboxylase domain of single-chain bacterial carboxylase

PDB ID 5h80

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