6rut: Difference between revisions
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==Mycoplasma Genitalium Heterodimer Nap Complex (P140-P110 globular)== | |||
<StructureSection load='6rut' size='340' side='right'caption='[[6rut]], [[Resolution|resolution]] 2.65Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6rut]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycoplasma_genitalium_G37 Mycoplasma genitalium G37]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RUT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RUT 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]] 2.65Å</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=6rut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rut OCA], [https://pdbe.org/6rut PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rut RCSB], [https://www.ebi.ac.uk/pdbsum/6rut PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rut ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/MGP3_MYCGE MGP3_MYCGE] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Mycoplasma genitalium is a human pathogen adhering to host target epithelial cells and causing urethritis, cervicitis and pelvic inflammatory disease. Essential for infectivity is a transmembrane adhesion complex called Nap comprising proteins P110 and P140. Here we report the crystal structure of P140 both alone and in complex with the N-terminal domain of P110. By cryo-electron microscopy (cryo-EM) and tomography (cryo-ET) we find closed and open Nap conformations, determined at 9.8 and 15 A, respectively. Both crystal structures and the cryo-EM structure are found in a closed conformation, where the sialic acid binding site in P110 is occluded. By contrast, the cryo-ET structure shows an open conformation, where the binding site is accessible. Structural information, in combination with functional studies, suggests a mechanism for attachment and release of M. genitalium to and from the host cell receptor, in which Nap conformations alternate to sustain motility and guarantee infectivity. | |||
Structure and mechanism of the Nap adhesion complex from the human pathogen Mycoplasma genitalium.,Aparicio D, Scheffer MP, Marcos-Silva M, Vizarraga D, Sprankel L, Ratera M, Weber MS, Seybert A, Torres-Puig S, Gonzalez-Gonzalez L, Reitz J, Querol E, Pinol J, Pich OQ, Fita I, Frangakis AS Nat Commun. 2020 Jun 8;11(1):2877. doi: 10.1038/s41467-020-16511-2. PMID:32513917<ref>PMID:32513917</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6rut" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Adhesin 3D structures|Adhesin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mycoplasma genitalium G37]] | |||
[[Category: Aparicio D]] | |||
[[Category: Fita I]] | |||
Latest revision as of 12:29, 24 January 2024
Mycoplasma Genitalium Heterodimer Nap Complex (P140-P110 globular)
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