3hjt | pdb_00003hjt

Structure of laminin binding protein (Lmb) of Streptococcus agalactiae A bifunctional protein with adhesin and metal transporting activity

spinqualitylabelsall models 3hjt, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3hjt is a 2 chain structure with sequence from "streptoccocus_de_la_mammite"_nocard_and_mollereau_1887 "streptoccocus de la mammite" nocard and mollereau 1887. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ZN Gene: lmb ("Streptoccocus de la mammite" Nocard and Mollereau 1887) Resources: FirstGlance, OCA, RCSB, PDBsum 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 Adhesion/invasion of pathogenic bacteria is a critical step in infection and is mediated by surface-exposed proteins termed adhesins. The crystal structure of recombinant Lmb, a laminin-binding adhesin from Streptococcus agalactiae, has been determined at 2.5 A resolution. Based on sequence and structural homology, Lmb was placed into the cluster 9 family of the ABC (ATP-binding cassette) transport system. The structural organization of Lmb closely resembles that of ABC-type solute-binding proteins (SBPs), in which two structurally related globular domains interact with each other to form a metal-binding cavity at the interface. The bound zinc in Lmb is tetrahedrally coordinated by three histidines and a glutamate from both domains. A comparison of Lmb with other metal transporters revealed an interesting feature of the dimerization of molecules in the crystallographic asymmetric unit in all zinc-binding transporters. A closer comparison of Lmb with the zinc-binding ZnuA from Escherichia coli and Synechocystis 6803 suggested that Lmb might undergo a unique structural rearrangement upon metal binding and release. The crystal structure of Lmb provides an impetus for further investigations into the molecular basis of laminin binding by human pathogens. Being ubiquitous in all serotypes of group B streptococcus (GBS), the structure of Lmb may direct the development of an efficient vaccine. Structure of laminin-binding adhesin (Lmb) from Streptococcus agalactiae.,Ragunathan P, Spellerberg B, Ponnuraj K Acta Crystallogr D Biol Crystallogr. 2009 Dec;65(Pt 12):1262-9. doi:, 10.1107/S0907444909038359. Epub 2009 Nov 17. PMID:19966412 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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