3cg3

Crystal structure of P. horikoshii periplasmic binding protein ModA/WtpA with bound tungstateCrystal structure of P. horikoshii periplasmic binding protein ModA/WtpA with bound tungstate

Structural highlights 3cg3 is a 1 chain structure with sequence from 'pyrococcus shinkaii'. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: Related: 2onr, 3cfx, 3cg1 Gene: modA ('Pyrococcus shinkaii') Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [WTPA_PYRHO] Part of the ABC transporter complex WtpABC involved in molybdate/tungstate import. Binds tungstate and molybdate (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Bacteria and archaea import molybdenum and tungsten from the environment in the form of the oxyanions molybdate (MoO(4) (2-)) and tungstate (WO(4) (2-)). These substrates are captured by an external, high-affinity binding protein, and delivered to ATP binding cassette transporters, which move them across the cell membrane. We have recently reported a crystal structure of the molybdate/tungstate binding protein ModA/WtpA from Archaeoglobus fulgidus, which revealed an octahedrally coordinated central metal atom. By contrast, the previously determined structures of three bacterial homologs showed tetracoordinate molybdenum and tungsten atoms in their binding pockets. Until then, coordination numbers above four had only been found for molybdenum/tungsten in metalloenzymes where these metal atoms are part of the catalytic cofactors and coordinated by mostly non-oxygen ligands. We now report a high-resolution structure of A. fulgidus ModA/WtpA, as well as crystal structures of four additional homologs, all bound to tungstate. These crystal structures match X-ray absorption spectroscopy measurements from soluble, tungstate-bound protein, and reveal the details of the distorted octahedral coordination. Our results demonstrate that the distorted octahedral geometry is not an exclusive feature of the A. fulgidus protein, and suggest distinct binding modes of the binding proteins from archaea and bacteria. Distorted octahedral coordination of tungstate in a subfamily of specific binding proteins.,Hollenstein K, Comellas-Bigler M, Bevers LE, Feiters MC, Meyer-Klaucke W, Hagedoorn PL, Locher KP J Biol Inorg Chem. 2009 Feb 21. PMID:19234723 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also ABC transporter

spinqualitylabelsall models 3cg3, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image