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4qq1
From Proteopedia
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| - | ''' | + | ==Crystal structure of the isotype 1 Transferrin binding protein B (TbpB) from serogroup B Neisseria meningitidis== |
| + | <StructureSection load='4qq1' size='340' side='right' caption='[[4qq1]], [[Resolution|resolution]] 3.33Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4qq1]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QQ1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QQ1 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CS:CESIUM+ION'>CS</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4qq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qq1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qq1 RCSB], [http://www.ebi.ac.uk/pdbsum/4qq1 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/TBB2_NEIMI TBB2_NEIMI]] Acts as a transferrin receptor and is required for transferrin utilization. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:25800619</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
[[Category: Calmettes, C]] | [[Category: Calmettes, C]] | ||
| + | [[Category: Moraes, T F]] | ||
| + | [[Category: Host-pathogen interaction]] | ||
| + | [[Category: Iron acquisition]] | ||
| + | [[Category: Iron piracy]] | ||
| + | [[Category: Outer-membrane]] | ||
| + | [[Category: Protein binding]] | ||
| + | [[Category: Surface lipoprotein]] | ||
| + | [[Category: Transferrin binding]] | ||
| + | [[Category: Transferrin receptor]] | ||
| + | [[Category: Vaccine candidate]] | ||
Revision as of 13:14, 1 April 2015
Crystal structure of the isotype 1 Transferrin binding protein B (TbpB) from serogroup B Neisseria meningitidis
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