4r9u | pdb_00004r9u

Structure of vitamin B12 transporter BtuCD in a nucleotide-bound outward facing state

spinqualitylabelsall models 4r9u, resolution 2.79Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4r9u is a 4 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.785Å Ligands: ANP, LDA, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function BTUC_ECOLI Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Involved in the translocation of the substrate across the membrane.[HAMAP-Rule:MF_01004] 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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