5fif: Difference between revisions

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'''Unreleased structure'''


The entry 5fif is ON HOLD  until Paper Publication
==Carboxyltransferase domain of a single-chain bacterial carboxylase==
<StructureSection load='5fif' size='340' side='right' caption='[[5fif]], [[Resolution|resolution]] 2.49&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5fif]] is a 6 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FIF FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5fif FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fif OCA], [http://pdbe.org/5fif PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fif RCSB], [http://www.ebi.ac.uk/pdbsum/5fif PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fif ProSAT]</span></td></tr>
</table>
<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.


Authors:  
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>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 5fif" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Hagmann, A]]
[[Category: Hunkeler, M]]
[[Category: Maier, T]]
[[Category: Stuttfeld, E]]
[[Category: Carrier protein]]
[[Category: Ligase]]
[[Category: Multienzyme]]
[[Category: Protein dynamic]]
[[Category: Small-angle x-ray scattering]]
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