4qq1

Crystal structure of the isotype 1 Transferrin binding protein B (TbpB) from serogroup B Neisseria meningitidis

spinqualitylabelsall models 4qq1, resolution 3.33Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4qq1 is a 3 chain structure with sequence from Neisseria meningitidis serogroup B. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.33Å Ligands: CS, GOL, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TBPB2_NEIMI Neisseria acquires iron by extracting it from serum transferrin (TF) in its human host. Acts as a TF receptor and is required for TF utilization. Involved in the initial capture of TF. Helps select only those TF molecules that can be used as an iron source and concentrates them on the cell surface, maintaining the iron-loaded status of the TF C-terminal lobe until its delivery to TbpA.[UniProtKB:Q09057] Publication Abstract from PubMed Neisseria meningitidis inhabits the human upper respiratory tract and is an important cause of sepsis and meningitis. A surface receptor comprised of transferrin-binding proteins A and B (TbpA and TbpB), is responsible for acquiring iron from host transferrin. Sequence and immunological diversity divides TbpBs into two distinct lineages; isotype I and isotype II. Two representative isotype I and II strains, B16B6 and M982, differ in their dependence on TbpB for in vitro growth on exogenous transferrin. The crystal structure of TbpB and a structural model for TbpA from the representative isotype I N. meningitidis strain B16B6 were obtained. The structures were integrated with a comprehensive analysis of the sequence diversity of these proteins to probe for potential functional differences. A distinct isotype I TbpA was identified that co-varied with TbpB and lacked sequence in the region for the loop 3 alpha-helix that is proposed to be involved in iron removal from transferrin. The tightly associated isotype I TbpBs had a distinct anchor peptide region, a distinct, smaller linker region between the lobes and lacked the large loops in the isotype II C-lobe. Sequences of the intact TbpB, the TbpB N-lobe, the TbpB C-lobe, and TbpA were subjected to phylogenetic analyses. The phylogenetic clustering of TbpA and the TbpB C-lobe were similar with two main branches comprising the isotype 1 and isotype 2 TbpBs, possibly suggesting an association between TbpA and the TbpB C-lobe. The intact TbpB and TbpB N-lobe had 4 main branches, one consisting of the isotype 1 TbpBs. One isotype 2 TbpB cluster appeared to consist of isotype 1 N-lobe sequences and isotype 2 C-lobe sequences, indicating the swapping of N-lobes and C-lobes. Our findings should inform future studies on the interaction between TbpB and TbpA and the process of iron acquisition. Patterns of structural and sequence variation within isotype lineages of the Neisseria meningitidis transferrin receptor system.,Adamiak P, Calmettes C, Moraes TF, Schryvers AB Microbiologyopen. 2015 Mar 19. doi: 10.1002/mbo3.254. PMID:25800619 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Transferrin-binding protein

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