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8hc1
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8hc1]] is a 48 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=8HC1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HC1 FirstGlance]. <br> | <table><tr><td colspan='2'>[[8hc1]] is a 48 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=8HC1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HC1 FirstGlance]. <br> | ||
| - | </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=8hc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hc1 OCA], [https://pdbe.org/8hc1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hc1 RCSB], [https://www.ebi.ac.uk/pdbsum/8hc1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hc1 ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.3Å</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=8hc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hc1 OCA], [https://pdbe.org/8hc1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hc1 RCSB], [https://www.ebi.ac.uk/pdbsum/8hc1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hc1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/URE23_HELPY URE23_HELPY] Ammonia produced by ureolysis increases the gastric pH thereby providing an environment permissive for colonization of the stomach.<ref>PMID:8039935</ref> | [https://www.uniprot.org/uniprot/URE23_HELPY URE23_HELPY] Ammonia produced by ureolysis increases the gastric pH thereby providing an environment permissive for colonization of the stomach.<ref>PMID:8039935</ref> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Urease is a nickel (Ni) enzyme that is essential for the colonization of Helicobacter pylori in the human stomach. To solve the problem of delivering the toxic Ni ion to the active site without diffusing into the cytoplasm, cells have evolved metal carrier proteins, or metallochaperones, to deliver the toxic ions to specific protein complexes. Ni delivery requires urease to form an activation complex with the urease accessory proteins UreFD and UreG. Here, we determined the cryo-electron microscopy structures of H. pylori UreFD/urease and Klebsiella pneumoniae UreD/urease complexes at 2.3- and 2.7-angstrom resolutions, respectively. Combining structural, mutagenesis, and biochemical studies, we show that the formation of the activation complex opens a 100-angstrom-long tunnel, where the Ni ion is delivered through UreFD to the active site of urease. | ||
| - | + | ==See Also== | |
| - | + | *[[Urease accessory protein 3D structures|Urease accessory protein 3D structures]] | |
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== References == | == References == | ||
<references/> | <references/> | ||
Current revision
CryoEM structure of Helicobacter pylori UreFD/urease complex
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Categories: Helicobacter pylori 26695 | Large Structures | Caesar J | Deme J | Fong IYH | Johnson S | Lea SM | Nim YS | Tsang KL | Wong KB
