View source for 7cmg


==The Structure of the periplasmic domain of PorM==
<StructureSection load='7cmg' size='340' side='right'caption='[[7cmg]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7cmg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Porphyromonas_gingivalis_ATCC_33277 Porphyromonas gingivalis ATCC 33277]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CMG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CMG 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]] 3.7&#8491;</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=7cmg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cmg OCA], [https://pdbe.org/7cmg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cmg RCSB], [https://www.ebi.ac.uk/pdbsum/7cmg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cmg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B2RLE8_PORG3 B2RLE8_PORG3] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Porphyromonas gingivalis, which is a major pathogen of the periodontal disease, secrets virulence factors such as gingipain proteases via the type IX secretion system (T9SS). T9SS consists of a trans-periplasmic core complex, the outer membrane translocon complex and the cell-surface complex attached on the outer membrane. PorM is a major component of the trans-periplasmic core complex and is believed to connect the outer membrane component with the inner membrane component. Recent structural studies have revealed that the periplasmic region of GldM, a PorM homolog of a gliding bacterium, consist of four domains and forms a dimer with a straight rod shape. However, only fragment structures are known for PorM. Moreover, one of the PorM fragment structure shows a kink. Here we show the structure of the entire structure of the periplasmic region of PorM (PorMp) at 3.7 A resolution. PorMp is made up of four domains and forms a unique dimeric structure with an asymmetric, kinked-rod shape. The structure and the following mutational analysis revealed that R204 stabilizes the kink between the D1 and D2 domains and is essential for gingipains secretion, suggesting that the kinked structure of PorM is important for the functional T9SS formation.

PorM, a core component of bacterial type IX secretion system, forms a dimer with a unique kinked-rod shape.,Sato K, Okada K, Nakayama K, Imada K Biochem Biophys Res Commun. 2020 Aug 19. pii: S0006-291X(20)31563-1. doi:, 10.1016/j.bbrc.2020.08.018. PMID:32828535<ref>PMID:32828535</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7cmg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Porphyromonas gingivalis ATCC 33277]]
[[Category: Imada K]]
[[Category: Nakayam K]]
[[Category: Okada K]]
[[Category: Sato K]]