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==1.5 Angstrom crystal structure of a novel cobalamin-binding protein from Desulfitobacterium hafniense DCB-2== | |||
<StructureSection load='4jgi' size='340' side='right' caption='[[4jgi]], [[Resolution|resolution]] 1.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4jgi]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Desulfitobacterium_hafniense Desulfitobacterium hafniense]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JGI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JGI FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COB:CO-METHYLCOBALAMIN'>COB</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=4jgi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jgi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4jgi RCSB], [http://www.ebi.ac.uk/pdbsum/4jgi PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
This study describes the identification and the structural and spectroscopic analysis of a cobalamin-binding protein (termed CobDH) implicated in O-demethylation by the organohalide-respiring bacterium Desulfitobacterium hafniense DCB-2. The 1.5 A resolution crystal structure of CobDH is presented in the cobalamin-bound state and reveals that the protein is composed of an N-terminal helix-bundle domain and a C-terminal Rossmann-fold domain, with the cobalamin coordinated in the base-off/His-on conformation similar to other cobalamin-binding domains that catalyse methyl-transfer reactions. EPR spectroscopy of CobDH confirms cobalamin binding and reveals the presence of a cob(III)alamin superoxide, indicating binding of oxygen to the fully oxidized cofactor. These data provide the first structural insights into the methyltransferase reactions that occur during O-demethylation by D. hafniense. | |||
Structure of the cobalamin-binding protein of a putative O-demethylase from Desulfitobacterium hafniense DCB-2.,Sjuts H, Dunstan MS, Fisher K, Leys D Acta Crystallogr D Biol Crystallogr. 2013 Aug;69(Pt 8):1609-16. doi:, 10.1107/S0907444913011323. Epub 2013 Jul 20. PMID:23897483<ref>PMID:23897483</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Desulfitobacterium hafniense]] | [[Category: Desulfitobacterium hafniense]] | ||
[[Category: Dunstan, M S | [[Category: Dunstan, M S]] | ||
[[Category: Fisher, K | [[Category: Fisher, K]] | ||
[[Category: Leys, D | [[Category: Leys, D]] | ||
[[Category: Sjuts, H | [[Category: Sjuts, H]] | ||
[[Category: Cobalamin]] | [[Category: Cobalamin]] | ||
[[Category: Cobalamin binding]] | [[Category: Cobalamin binding]] | ||
[[Category: Protein binding]] | [[Category: Protein binding]] | ||
[[Category: Rossmann fold]] | [[Category: Rossmann fold]] | ||
Revision as of 09:31, 22 January 2015
1.5 Angstrom crystal structure of a novel cobalamin-binding protein from Desulfitobacterium hafniense DCB-21.5 Angstrom crystal structure of a novel cobalamin-binding protein from Desulfitobacterium hafniense DCB-2
Structural highlights
Publication Abstract from PubMedThis study describes the identification and the structural and spectroscopic analysis of a cobalamin-binding protein (termed CobDH) implicated in O-demethylation by the organohalide-respiring bacterium Desulfitobacterium hafniense DCB-2. The 1.5 A resolution crystal structure of CobDH is presented in the cobalamin-bound state and reveals that the protein is composed of an N-terminal helix-bundle domain and a C-terminal Rossmann-fold domain, with the cobalamin coordinated in the base-off/His-on conformation similar to other cobalamin-binding domains that catalyse methyl-transfer reactions. EPR spectroscopy of CobDH confirms cobalamin binding and reveals the presence of a cob(III)alamin superoxide, indicating binding of oxygen to the fully oxidized cofactor. These data provide the first structural insights into the methyltransferase reactions that occur during O-demethylation by D. hafniense. Structure of the cobalamin-binding protein of a putative O-demethylase from Desulfitobacterium hafniense DCB-2.,Sjuts H, Dunstan MS, Fisher K, Leys D Acta Crystallogr D Biol Crystallogr. 2013 Aug;69(Pt 8):1609-16. doi:, 10.1107/S0907444913011323. Epub 2013 Jul 20. PMID:23897483[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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