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1e9z

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Revision as of 22:14, 9 September 2015

CRYSTAL STRUCTURE OF HELICOBACTER PYLORI UREASE

Structural highlights

1e9z is a 2 chain structure with sequence from Atcc 43504. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Related:	1e9y
Activity:	Urease, with EC number 3.5.1.5
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[URE23_HELPY] Ammonia produced by ureolysis increases the gastric pH thereby providing an environment permissive for colonization of the stomach.^[1] [URE1_HELPY] Ammonia produced by ureolysis increases the gastric pH thereby providing an environment permissive for colonization of the stomach.^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Helicobacter pylori, an etiologic agent in a variety of gastroduodenal diseases, produces a large amount of urease, which is believed to neutralize gastric acid by producing ammonia for the survival of the bacteria. Up to 30% of the enzyme associates with the surface of intact cells upon lysis of neighboring bacteria. The role of the enzyme at the extracellular location has been a subject of controversy because the purified enzyme is irreversibly inactivated below pH 5. We have determined the crystal structure of H. pylori urease, which has a 1.1 MDa spherical assembly of 12 catalytic units with an outer diameter of approximately 160 A. Under physiologically relevant conditions, the activity of the enzyme remains unaffected down to pH 3. Activity assays under different conditions indicated that the cluster of the 12 active sites on the supramolecular assembly may be critical for the survival of the enzyme at low pH. The structure provides a novel example of a molecular assembly adapted for acid resistance that, together with the low Km value of the enzyme, is likely to enable the organism to inhabit the hostile niche.

Supramolecular assembly and acid resistance of Helicobacter pylori urease.,Ha NC, Oh ST, Sung JY, Cha KA, Lee MH, Oh BH Nat Struct Biol. 2001 Jun;8(6):505-9. PMID:11373617^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Tsuda M, Karita M, Morshed MG, Okita K, Nakazawa T. A urease-negative mutant of Helicobacter pylori constructed by allelic exchange mutagenesis lacks the ability to colonize the nude mouse stomach. Infect Immun. 1994 Aug;62(8):3586-9. PMID:8039935
↑ Tsuda M, Karita M, Morshed MG, Okita K, Nakazawa T. A urease-negative mutant of Helicobacter pylori constructed by allelic exchange mutagenesis lacks the ability to colonize the nude mouse stomach. Infect Immun. 1994 Aug;62(8):3586-9. PMID:8039935
↑ Ha NC, Oh ST, Sung JY, Cha KA, Lee MH, Oh BH. Supramolecular assembly and acid resistance of Helicobacter pylori urease. Nat Struct Biol. 2001 Jun;8(6):505-9. PMID:11373617 doi:10.1038/88563

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1e9z"

@@ Line 2: / Line 2: @@
 <StructureSection load='1e9z' size='340' side='right' caption='[[1e9z]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1e9z]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E9Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E9Z FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1e9z]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43504 Atcc 43504]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E9Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E9Z FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1e9y|1e9y]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Urease Urease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.5 3.5.1.5] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e9z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e9z OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e9z RCSB], [http://www.ebi.ac.uk/pdbsum/1e9z PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e9z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e9z OCA], [http://pdbe.org/1e9z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e9z RCSB], [http://www.ebi.ac.uk/pdbsum/1e9z PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 29: / Line 29: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1e9z" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 36: / Line 37: @@
 __TOC__
 </StructureSection>
-[[Category: Helicobacter pylori]]
+[[Category: Atcc 43504]]
 [[Category: Urease]]
 [[Category: Ha, N C]]

1e9z

From Proteopedia

Revision as of 22:14, 9 September 2015

CRYSTAL STRUCTURE OF HELICOBACTER PYLORI UREASE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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