2mpb

NMR structure of BA42 protein from the psychrophilic bacteria Bizionia argentinensis sp. nov

spinqualitylabelsall models 2mpb Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2mpb is a 1 chain structure with sequence from Bizionia argentinensis JUB59. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G2EA45_9FLAO Publication Abstract from PubMed The structure of the BA42 protein belonging to the Antarctic flavobacterium Bizionia argentinensis was determined by Nuclear Magnetic Resonance and X-ray crystallography. This is the first structure of a member of the PF04536 family comprised of a stand-alone TPM domain. The structure reveals a new topological variant of the four beta-strands constituting the central beta-sheet of the alphabetaalpha architecture and a double metal binding site stabilizing a pair of crossing loops, not observed in previous structures of proteins belonging to this family. BA42 shows differences in structure and dynamics in the presence or absence of bound metals. The affinity for divalent metal ions is close to that observed in proteins that modulate their activity as a function of metal concentration, anticipating a possible role for BA42. (c) Proteins 2014;. (c) 2014 Wiley Periodicals, Inc. Solution and crystal structure of BA42, a protein from the Antarctic bacterium Bizionia argentinensis comprised of a stand-alone TPM domain.,Aran M, Smal C, Pellizza L, Gallo M, Otero LH, Klinke S, Goldbaum FA, Ithurralde ER, Bercovich A, Mac Cormack WP, Turjanski AG, Cicero DO Proteins. 2014 Aug 13. doi: 10.1002/prot.24667. PMID:25116514 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Acid phosphatase 3D structures BA42

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