3lzl

Crystal Structure Analysis of the as-solated P19 protein from Campylobacter jejuni at 1.45 A at pH 9.0

spinqualitylabelsall models 3lzl, resolution 1.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3lzl is a 2 chain structure with sequence from Camjj. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CU, SO4 Related: 2o6c, 2o6d, 2o6e, 2o6f, 3lzo, 3lzp, 3lzq, 3lzn, 3lzr Gene: CJJ81176_1650, Gene Cj81176_1659 (CAMJJ) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 Campylobacter jejuni, a major cause of acute bacterial diarrhea in humans, expresses numerous proteins to import diverse forms of essential iron. The expression of p19 and an adjacent iron transporter homologue (ftr1) is strongly induced upon iron limitation, suggesting a function in iron acquisition. Here, we show that the loss of P19 alone is detrimental to growth on iron-restricted media. Furthermore, metal binding analysis demonstrates that recombinant P19 has distinct copper and iron binding sites. Crystal structures of P19 have been solved to 1.41 A resolution, revealing an immunoglobulin-like fold. A P19 homodimer in which both monomers contribute ligands to two equivalent copper sites located adjacent to methionine-rich patches is observed. Copper coordination occurs via three histidine residues (His42, His95, and His132) and Met88. A solvent channel lined with conserved acidic residues leads to the copper site. Soaking crystals with a solution of manganese as iron analog reveals a second metal binding site in this solvent channel (metal-metal distance, 7.7 A). Glu44 lies between the metal sites and displays multiple conformations in the crystal structures, suggesting a role in regulating metal-metal interaction. Dimerization is shown to be metal dependent in vitro and is detected in vivo by cross-linking. Structure and function of P19, a high-affinity iron transporter of the human pathogen Campylobacter jejuni.,Chan AC, Doukov TI, Scofield M, Tom-Yew SA, Ramin AB, Mackichan JK, Gaynor EC, Murphy ME J Mol Biol. 2010 Aug 27;401(4):590-604. Epub 2010 Jun 30. PMID:20600116 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also P19

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