6yrk
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 6yrk is ON HOLD until Paper Publication Authors: Scheffer, M.P., Aparicio, D. Description: P140-P110 complex fitted into the cryo-electron density ...) |
|||
| (2 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==P140-P110 complex fitted into the cryo-electron density map of the heterodimer== | |
| + | <StructureSection load='6yrk' size='340' side='right'caption='[[6yrk]], [[Resolution|resolution]] 4.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6yrk]] is a 2 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=6YRK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YRK FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.1Å</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=6yrk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yrk OCA], [https://pdbe.org/6yrk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6yrk RCSB], [https://www.ebi.ac.uk/pdbsum/6yrk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6yrk 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> |
| - | [[Category: Aparicio | + | <div class="pdbe-citations 6yrk" style="background-color:#fffaf0;"></div> |
| - | [[Category: Scheffer | + | |
| + | ==See Also== | ||
| + | *[[Adhesin 3D structures|Adhesin 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mycoplasma genitalium G37]] | ||
| + | [[Category: Aparicio D]] | ||
| + | [[Category: Scheffer MP]] | ||
Current revision
P140-P110 complex fitted into the cryo-electron density map of the heterodimer
| |||||||||||
