3ve2: Difference between revisions
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The | ==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 [https://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 [https://proteopedia.org/fgij/fg.htm?mol=3VE2 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.14Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ve2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ve2 OCA], [https://pdbe.org/3ve2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ve2 RCSB], [https://www.ebi.ac.uk/pdbsum/3ve2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ve2 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/TBPB1_NEIMI TBPB1_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.<ref>PMID:22343719</ref> | |||
<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> | |||
<div class="pdbe-citations 3ve2" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Transferrin-binding protein|Transferrin-binding protein]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Neisseria meningitidis serogroup B]] | |||
[[Category: Calmettes C]] | |||
[[Category: Moraes TF]] | |||
Latest revision as of 13:33, 6 November 2024
The 2.1 angstrom crystal structure of Transferrin binding protein B (TbpB) from serogroup B M982 Neisseria meningitidisThe 2.1 angstrom crystal structure of Transferrin binding protein B (TbpB) from serogroup B M982 Neisseria meningitidis
Structural highlights
FunctionTBPB1_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.[1] Publication Abstract from PubMedNeisseria 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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