5fif
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Carboxyltransferase domain of a single-chain bacterial carboxylase== | |
| + | <StructureSection load='5fif' size='340' side='right'caption='[[5fif]], [[Resolution|resolution]] 2.49Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5fif]] is a 6 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=5FIF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FIF FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.494Å</td></tr> | ||
| + | <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> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5fif FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fif OCA], [https://pdbe.org/5fif PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fif RCSB], [https://www.ebi.ac.uk/pdbsum/5fif PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fif ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q9RYK2_DEIRA Q9RYK2_DEIRA] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5fif" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Deinococcus radiodurans]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Hagmann A]] | ||
| + | [[Category: Hunkeler M]] | ||
| + | [[Category: Maier T]] | ||
| + | [[Category: Stuttfeld E]] | ||
Current revision
Carboxyltransferase domain of a single-chain bacterial carboxylase
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