2jv7: Difference between revisions
New page: '''Unreleased structure''' The entry 2jv7 is ON HOLD until Paper Publication Authors: Beck, M.R., DeKoster, G.T., Cistola, D.P., Goldman, W.E. Description: NMR Solution Structure of Hi... |
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==NMR Solution Structure of Histoplasma capsulatum CBP Homodimer== | |||
<StructureSection load='2jv7' size='340' side='right'caption='[[2jv7]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2jv7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Histoplasma_capsulatum Histoplasma capsulatum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JV7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JV7 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=2jv7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jv7 OCA], [https://pdbe.org/2jv7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jv7 RCSB], [https://www.ebi.ac.uk/pdbsum/2jv7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jv7 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CBP1_AJECG CBP1_AJECG] Involved in calcium binding and uptake in yeast phase. Required for growth in limiting calcium conditions and for yeast survival in host macrophages. Is able to bind a variety of lipids.<ref>PMID:11082066</ref> <ref>PMID:19298372</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The fungal protein CBP (calcium binding protein) is a known virulence factor with an unknown virulence mechanism. The protein was identified based on its ability to bind calcium and its prevalence as Histoplasma capsulatum's most abundant secreted protein. However, CBP has no sequence homology with other CBPs and contains no known calcium binding motifs. Here, the NMR structure of CBP reveals a highly intertwined homodimer and represents the first atomic level NMR model of any fungal virulence factor. Each CBP monomer is comprised of four alpha-helices that adopt the saposin fold, characteristic of a protein family that binds to membranes and lipids. This structural homology suggests that CBP functions as a lipid binding protein, potentially interacting with host glycolipids in the phagolysosome of host cells. | |||
NMR structure of a fungal virulence factor reveals structural homology with mammalian saposin B.,Beck MR, Dekoster GT, Cistola DP, Goldman WE Mol Microbiol. 2009 Apr;72(2):344-53. Epub 2009 Mar 3. PMID:19298372<ref>PMID:19298372</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2jv7" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Histoplasma capsulatum]] | |||
[[Category: Large Structures]] | |||
[[Category: Beck MR]] | |||
[[Category: Cistola DP]] | |||
[[Category: DeKoster GT]] | |||
[[Category: Goldman WE]] | |||