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Article: Urease inactivation by an unusual GroES chaperonin

TitleUrease inactivation by an unusual GroES chaperonin
Authors
Issue Date2014
PublisherScience China Press, co-published with Springer. The Journal's web site is located at http://chem.scichina.com:8081/sciBe/EN/volumn/current.shtml
Citation
Science China Chemistry, 2014, v. 57 n. 6, p. 842-848 How to Cite?
AbstractIt remains uncovered yet how the common gastric pathogen, Helicobacter pylori, survives through the acidic barrier and the immune response simultaneously in the stomach. Herein we report a unique GroES chaperonin that effectively inactivates Helicobacter pylori urease in Escherichia coli model. Such a function depends on the quaternary structure as well as the metal binding at the C terminus. Surprisingly, the C-terminal metal capacity seems not closely relevant to the apparent urease inactivation. Our findings have possibly revealed a survival strategy of Helicobacter pylori after its gastric localization. © 2014 Science China Press and Springer-Verlag Berlin Heidelberg.
Persistent Identifierhttp://hdl.handle.net/10722/202608
ISSN
2015 Impact Factor: 2.429
2015 SCImago Journal Rankings: 0.567
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorCun, SJ-
dc.contributor.authorSun, H-
dc.date.accessioned2014-09-19T08:42:29Z-
dc.date.available2014-09-19T08:42:29Z-
dc.date.issued2014-
dc.identifier.citationScience China Chemistry, 2014, v. 57 n. 6, p. 842-848-
dc.identifier.issn1674-7291-
dc.identifier.urihttp://hdl.handle.net/10722/202608-
dc.description.abstractIt remains uncovered yet how the common gastric pathogen, Helicobacter pylori, survives through the acidic barrier and the immune response simultaneously in the stomach. Herein we report a unique GroES chaperonin that effectively inactivates Helicobacter pylori urease in Escherichia coli model. Such a function depends on the quaternary structure as well as the metal binding at the C terminus. Surprisingly, the C-terminal metal capacity seems not closely relevant to the apparent urease inactivation. Our findings have possibly revealed a survival strategy of Helicobacter pylori after its gastric localization. © 2014 Science China Press and Springer-Verlag Berlin Heidelberg.-
dc.languageeng-
dc.publisherScience China Press, co-published with Springer. The Journal's web site is located at http://chem.scichina.com:8081/sciBe/EN/volumn/current.shtml-
dc.relation.ispartofScience China Chemistry-
dc.rightsThe original publication is available at www.scichina.com and www.springerlink.com-
dc.titleUrease inactivation by an unusual GroES chaperonin-
dc.typeArticle-
dc.identifier.emailSun, H: hsun@hku.hk-
dc.identifier.authoritySun, H=rp00777-
dc.identifier.doi10.1007/s11426-014-5088-9-
dc.identifier.scopuseid_2-s2.0-84902266824-
dc.identifier.hkuros239334-
dc.identifier.volume57-
dc.identifier.issue6-
dc.identifier.spage842-
dc.identifier.epage848-
dc.identifier.isiWOS:000336747700007-
dc.publisher.placeChina-

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