4r9u
From Proteopedia
(Difference between revisions)
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<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=4r9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r9u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r9u RCSB], [http://www.ebi.ac.uk/pdbsum/4r9u PDBsum]</span></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=4r9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r9u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r9u RCSB], [http://www.ebi.ac.uk/pdbsum/4r9u PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The reaction mechanism of BtuCD-F-catalyzed vitamin B12 transport into Escherichia coli is currently unclear. Here we present the structure of the last missing state in the form of AMP-PNP-bound BtuCD, trapped by a disulfide cross-link. Our structural and biochemical data allow a consistent mechanism to be formulated, thus rationalizing the roles of substrate, ATP and substrate-binding protein. | ||
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| + | Structure of AMP-PNP-bound BtuCD and mechanism of ATP-powered vitamin B12 transport by BtuCD-F.,Korkhov VM, Mireku SA, Veprintsev DB, Locher KP Nat Struct Mol Biol. 2014 Nov 17. doi: 10.1038/nsmb.2918. PMID:25402482<ref>PMID:25402482</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 07:35, 3 December 2014
Structure of vitamin B12 transporter BtuCD in a nucleotide-bound outward facing state
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