View source for 6rut


==Mycoplasma Genitalium Heterodimer Nap Complex (P140-P110 globular)==
<StructureSection load='6rut' size='340' side='right'caption='[[6rut]], [[Resolution|resolution]] 2.65&Aring;' 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]] 2.65&#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=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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6rut" style="background-color:#fffaf0;"></div>

==See Also==
*[[Adhesin 3D structures|Adhesin 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Mycoplasma genitalium G37]]
[[Category: Aparicio D]]
[[Category: Fita I]]