6e6a: Difference between revisions

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'''Unreleased structure'''


The entry 6e6a is ON HOLD
==Triclinic crystal form of IncA G144A point mutant==
<StructureSection load='6e6a' size='340' side='right'caption='[[6e6a]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6e6a]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlamydia_trachomatis Chlamydia trachomatis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E6A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6E6A 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]] 1.95&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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=6e6a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e6a OCA], [https://pdbe.org/6e6a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6e6a RCSB], [https://www.ebi.ac.uk/pdbsum/6e6a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6e6a ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/INCA_CHLTR INCA_CHLTR] Chlamydia replicate within an intracellular vacuole, termed an inclusion. IncA is probably involved in the homotypic fusion of inclusions.[UniProtKB:A0A0H3MD02]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Many intracellular bacteria, including Chlamydia, establish a parasitic membrane-bound organelle inside the host cell that is essential for the bacteria's survival. Chlamydia trachomatis forms inclusions that are decorated with poorly characterized membrane proteins known as Incs. The prototypical Inc, called IncA, enhances Chlamydia pathogenicity by promoting the homotypic fusion of inclusions and shares structural and functional similarity to eukaryotic SNAREs. Here, we present the atomic structure of the cytoplasmic domain of IncA, which reveals a non-canonical four-helix bundle. Structure-based mutagenesis, molecular dynamics simulation, and functional cellular assays identify an intramolecular clamp that is essential for IncA-mediated homotypic membrane fusion during infection.


Authors: Cingolani, G., Paumet, F.
Structural basis for the homotypic fusion of chlamydial inclusions by the SNARE-like protein IncA.,Cingolani G, McCauley M, Lobley A, Bryer AJ, Wesolowski J, Greco DL, Lokareddy RK, Ronzone E, Perilla JR, Paumet F Nat Commun. 2019 Jun 21;10(1):2747. doi: 10.1038/s41467-019-10806-9. PMID:31227715<ref>PMID:31227715</ref>


Description: Triclinic crystal form of IncA G144A point mutant
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Cingolani, G]]
<div class="pdbe-citations 6e6a" style="background-color:#fffaf0;"></div>
[[Category: Paumet, F]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Chlamydia trachomatis]]
[[Category: Large Structures]]
[[Category: Cingolani G]]
[[Category: Paumet F]]

Latest revision as of 06:19, 11 October 2023

Triclinic crystal form of IncA G144A point mutant

6e6a, resolution 1.95Å

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