3ve2
From Proteopedia
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| - | [[ | + | ==The 2.1 angstrom crystal structure of Transferrin binding protein B (TbpB) from serogroup B M982 Neisseria meningitidis== |
| + | <StructureSection load='3ve2' size='340' side='right' caption='[[3ve2]], [[Resolution|resolution]] 2.14Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3ve2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Neisseria_meningitidis_serogroup_b Neisseria meningitidis serogroup b]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VE2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VE2 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ve1|3ve1]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tbpB, tbp2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=491 Neisseria meningitidis serogroup B])</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=3ve2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ve2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ve2 RCSB], [http://www.ebi.ac.uk/pdbsum/3ve2 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Neisseria meningitidis, the causative agent of bacterial meningitis, acquires the essential element iron from the host glycoprotein transferrin during infection through a surface transferrin receptor system composed of proteins TbpA and TbpB. Here we present the crystal structures of TbpB from N. meningitidis in its apo form and in complex with human transferrin. The structure reveals how TbpB sequesters and initiates iron release from human transferrin. | ||
| - | + | The structural basis of transferrin sequestration by transferrin-binding protein B.,Calmettes C, Alcantara J, Yu RH, Schryvers AB, Moraes TF Nat Struct Mol Biol. 2012 Feb 19;19(3):358-60. doi: 10.1038/nsmb.2251. PMID:22343719<ref>PMID:22343719</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | == | + | __TOC__ |
| - | + | </StructureSection> | |
[[Category: Neisseria meningitidis serogroup b]] | [[Category: Neisseria meningitidis serogroup b]] | ||
| - | [[Category: Calmettes, C | + | [[Category: Calmettes, C]] |
| - | [[Category: Moraes, T F | + | [[Category: Moraes, T F]] |
[[Category: Beta barrel]] | [[Category: Beta barrel]] | ||
[[Category: Host pathogen interaction]] | [[Category: Host pathogen interaction]] | ||
Revision as of 10:53, 4 January 2015
The 2.1 angstrom crystal structure of Transferrin binding protein B (TbpB) from serogroup B M982 Neisseria meningitidis
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