4oku: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
== | ==Structure of Toxoplasma gondii proMIC2== | ||
[[4oku]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Toxgo Toxgo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OKU OCA]. | <StructureSection load='4oku' size='340' side='right' caption='[[4oku]], [[Resolution|resolution]] 3.20Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4oku]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Toxgo Toxgo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OKU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OKU FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4okr|4okr]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TGVEG_201780 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5811 TOXGO])</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=4oku FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oku OCA], [http://pdbe.org/4oku PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4oku RCSB], [http://www.ebi.ac.uk/pdbsum/4oku PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4oku ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Micronemal protein 2 (MIC2) is the key adhesin that supports gliding motility and host cell invasion by Toxoplasma gondii. With a von Willebrand factor A (VWA) domain and six thrombospondin repeat domains (TSR1-6) in its ectodomain, MIC2 connects to the parasite actomyosin system through its cytoplasmic tail. MIC2-associated protein (M2AP) binds noncovalently to the MIC2 ectodomain. MIC2 and M2AP are stored in micronemes as proforms. We find that the MIC2-M2AP ectodomain complex is a highly elongated 1:1 monomer with M2AP bound to the TSR6 domain. Crystal structures of N-terminal fragments containing the VWA and TSR1 domains for proMIC2 and MIC2 reveal a closed conformation of the VWA domain and how it associates with the TSR1 domain. A long, proline-rich, disulfide-bonded pigtail loop in TSR1 overlaps the VWA domain. Mannose alpha-C-linked to Trp-276 in TSR1 has an unusual (1)C4 chair conformation. The MIC2 VWA domain includes a mobile alpha5-helix and a 22-residue disordered region containing two disulfide bonds in place of an alpha6-helix. A hydrophobic residue in the prodomain binds to a pocket adjacent to the alpha7-helix that pistons in opening of the VWA domain to a putative high-affinity state. | |||
Structures of the Toxoplasma gliding motility adhesin.,Song G, Springer TA Proc Natl Acad Sci U S A. 2014 Apr 1;111(13):4862-7. doi:, 10.1073/pnas.1403059111. Epub 2014 Mar 17. PMID:24639528<ref>PMID:24639528</ref> | |||
<ref | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4oku" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Toxgo]] | [[Category: Toxgo]] | ||
[[Category: Song, G | [[Category: Song, G]] | ||
[[Category: Springer, T A | [[Category: Springer, T A]] | ||
[[Category: Adhesin]] | [[Category: Adhesin]] | ||
[[Category: Cell adhesion]] | [[Category: Cell adhesion]] | ||
Revision as of 17:08, 2 January 2017
Structure of Toxoplasma gondii proMIC2
| ||||||||||||
