2pt7: Difference between revisions

<table><tr><td colspan='2'>[[2pt7]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_26695 Helicobacter pylori 26695]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PT7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PT7 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]] 2.4&#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=2pt7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pt7 OCA], [https://pdbe.org/2pt7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pt7 RCSB], [https://www.ebi.ac.uk/pdbsum/2pt7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pt7 ProSAT]</span></td></tr>

    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pt/2pt7_consurf.spt"</scriptWhenChecked>

</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2pt7 ConSurf].

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Helicobacter pylori is one of the world's most successful human pathogens causing gastric ulcers and cancers. A key virulence factor of H. pylori is the Cag pathogenicity island, which encodes a type IV secretion system. HP0525 is an essential component of the Cag system and acts as an inner membrane associated ATPase. HP0525 forms double hexameric ring structures, with the C-terminal domains (CTDs) forming a closed ring and the N-terminal domains (NTDs) forming a dynamic, open ring. Here, the crystal structure of HP0525 in complex with a fragment of HP1451, a protein of previously unknown function, is reported. The HP1451 construct consists of two domains similar to nucleic acid-binding domains. Two HP1451 molecules bind to the HP0525 NTDs on opposite sides of the hexamer, locking it in the closed form and forming a partial lid over the HP0525 chamber. From the structure, it is suggested that HP1451 acts as an inhibitory factor of HP0525 to regulate Cag-mediated secretion, a suggestion confirmed by results of in vitro ATPase assay and in vivo pull-down experiments.

Identification, structure and mode of action of a new regulator of the Helicobacter pylori HP0525 ATPase.,Hare S, Fischer W, Williams R, Terradot L, Bayliss R, Haas R, Waksman G EMBO J. 2007 Nov 28;26(23):4926-34. Epub 2007 Nov 1. PMID:17972918<ref>PMID:17972918</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

</StructureSection>

[[Category: Helicobacter pylori 26695]]

[[Category: Large Structures]]

[[Category: Bayliss R]]

[[Category: Fischer W]]

[[Category: Haas R]]

[[Category: Hare S]]

[[Category: Terradot L]]

[[Category: Waksman G]]

[[Category: Williams R]]