4u9r | pdb_00004u9r

Structure of the N-terminal Extension from Cupriavidus metallidurans CzcP

spinqualitylabelsall models 4u9r, resolution 2.17Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4u9r is a 1 chain structure with sequence from Cupriavidus metallidurans CH34. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.17Å Ligands: CD, TCE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q1LAJ7_CUPMC Publication Abstract from PubMed The P1B-ATPases, which couple cation transport across membranes to ATP hydrolysis, are central to metal homeostasis in all organisms. An important feature of P1B-ATPases is the presence of soluble metal binding domains (MBDs) that regulate transport activity. Only one type of MBD has been characterized extensively, but bioinformatics analyses indicate that a diversity of MBDs may exist in nature. Here we report the biochemical, structural and functional characterization of a new MBD from the Cupriavidus metallidurans P1B-4-ATPase CzcP (CzcP MBD). The CzcP MBD binds two Cd2+, Co2+ or Zn2+ ions in distinct and unique sites and adopts an unexpected fold consisting of two fused ferredoxin-like domains. Both in vitro and in vivo activity assays using full-length CzcP, truncated CzcP and several variants indicate a regulatory role for the MBD and distinct functions for the two metal binding sites. Taken together, these findings elucidate a previously unknown MBD and suggest new regulatory mechanisms for metal transport by P1B-ATPases. A new metal binding domain involved in cadmium, cobalt and zinc transport.,Smith AT, Barupala D, Stemmler TL, Rosenzweig AC Nat Chem Biol. 2015 Jul 20. doi: 10.1038/nchembio.1863. PMID:26192600 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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