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Article: Structure of a nickel chaperone, HypA, from Helicobacter pylori reveals two distinct metal binding sites

TitleStructure of a nickel chaperone, HypA, from Helicobacter pylori reveals two distinct metal binding sites
Authors
Issue Date2009
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/jacsat/index.html
Citation
Journal Of The American Chemical Society, 2009, v. 131 n. 29, p. 10031-10040 How to Cite?
AbstractMetallochaperones bind metals and ensure the safe delivery of metals to the targets. They are required for the activation and maturation of nickel-containing enzymes [Ni,Fe]-hydrogenase and urease. Metallochaperone HypA was found to be essential to facilitate nickel delivery to hydrogenase together with its partner HypB, although the detailed mechanism is not clear. In this study, we have cloned hypA gene from Helicobacter pylori (strain 26695), overexpressed, and purified the protein. The zinc-bound HypA (Zn-HypA) exists as a monomer in solution, and its solution structure was determined by NMR spectroscopy together with molecular dynamics simulated annealing. Zn-HypA folds into two domains, including a zinc domain and a nickel domain with a mixed α/β structure. The former houses a rigid zinc-binding site possibly with the role of structural stabilization, whereas the latter harbors a nickel-binding site at the N-terminus. Zinc binds to the four conserved cysteines tetrahedrally as evidenced by 113Cd NMR spectroscopy, and nickel coordinates with four nitrogens of the protein probably in a square-planar geometry. Low coordination number of Ni2+ may allow the metal to be readily transferred to its downstream receptors. Our studies may shed light on how the metallochaperone exerts its functions in intracellular nickel delivery. © 2009 American Chemical Society.
Persistent Identifierhttp://hdl.handle.net/10722/157551
ISSN
2015 Impact Factor: 13.038
2015 SCImago Journal Rankings: 7.123
ISI Accession Number ID
Funding AgencyGrant Number
Council of Hong KongHKU7512/05M
HKU7042/07P
HKU7038/08P
RGC Collaborative Research FundHKU1/07C
HKU2/06C
UGC of Hong Kong SAR of China
University of Hong Kong
Funding Information:

We thank Research Grants Council of Hong Kong (HKU7512/05M, HKU7042/07P, HKU7038/08P), RGC Collaborative Research Fund (HKU1/07C and HKU2/06C), the UGC of Hong Kong SAR of China under the scheme of the Area of Excellence, and the University of Hong Kong for their support. We are grateful to Prof. John H. Viles (QMW, London) and Prof. Sunney Chan (Caltech) for helpful discussion and comments.

References

 

DC FieldValueLanguage
dc.contributor.authorXia, Wen_US
dc.contributor.authorLi, Hen_US
dc.contributor.authorSze, KHen_US
dc.contributor.authorSun, Hen_US
dc.date.accessioned2012-08-08T08:51:11Z-
dc.date.available2012-08-08T08:51:11Z-
dc.date.issued2009en_US
dc.identifier.citationJournal Of The American Chemical Society, 2009, v. 131 n. 29, p. 10031-10040en_US
dc.identifier.issn0002-7863en_US
dc.identifier.urihttp://hdl.handle.net/10722/157551-
dc.description.abstractMetallochaperones bind metals and ensure the safe delivery of metals to the targets. They are required for the activation and maturation of nickel-containing enzymes [Ni,Fe]-hydrogenase and urease. Metallochaperone HypA was found to be essential to facilitate nickel delivery to hydrogenase together with its partner HypB, although the detailed mechanism is not clear. In this study, we have cloned hypA gene from Helicobacter pylori (strain 26695), overexpressed, and purified the protein. The zinc-bound HypA (Zn-HypA) exists as a monomer in solution, and its solution structure was determined by NMR spectroscopy together with molecular dynamics simulated annealing. Zn-HypA folds into two domains, including a zinc domain and a nickel domain with a mixed α/β structure. The former houses a rigid zinc-binding site possibly with the role of structural stabilization, whereas the latter harbors a nickel-binding site at the N-terminus. Zinc binds to the four conserved cysteines tetrahedrally as evidenced by 113Cd NMR spectroscopy, and nickel coordinates with four nitrogens of the protein probably in a square-planar geometry. Low coordination number of Ni2+ may allow the metal to be readily transferred to its downstream receptors. Our studies may shed light on how the metallochaperone exerts its functions in intracellular nickel delivery. © 2009 American Chemical Society.en_US
dc.languageengen_US
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/jacsat/index.htmlen_US
dc.relation.ispartofJournal of the American Chemical Societyen_US
dc.subject.meshBacterial Proteins - Chemistry - Geneticsen_US
dc.subject.meshBinding Sitesen_US
dc.subject.meshComputer Simulationen_US
dc.subject.meshHelicobacter Pylori - Chemistry - Geneticsen_US
dc.subject.meshMagnetic Resonance Spectroscopyen_US
dc.subject.meshMetalloproteins - Chemistry - Geneticsen_US
dc.subject.meshModels, Chemicalen_US
dc.subject.meshModels, Molecularen_US
dc.subject.meshNickel - Chemistryen_US
dc.subject.meshProtein Structure, Secondaryen_US
dc.subject.meshReproducibility Of Resultsen_US
dc.titleStructure of a nickel chaperone, HypA, from Helicobacter pylori reveals two distinct metal binding sitesen_US
dc.typeArticleen_US
dc.identifier.emailSze, KH:khsze@hku.hken_US
dc.identifier.emailSun, H:hsun@hkucc.hku.hken_US
dc.identifier.authoritySze, KH=rp00785en_US
dc.identifier.authoritySun, H=rp00777en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1021/ja900543yen_US
dc.identifier.pmid19621959-
dc.identifier.scopuseid_2-s2.0-67651221840en_US
dc.identifier.hkuros163891-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-67651221840&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume131en_US
dc.identifier.issue29en_US
dc.identifier.spage10031en_US
dc.identifier.epage10040en_US
dc.identifier.eissn1520-5126-
dc.identifier.isiWOS:000268395000050-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridXia, W=40262950100en_US
dc.identifier.scopusauthoridLi, H=37063577200en_US
dc.identifier.scopusauthoridSze, KH=7006735061en_US
dc.identifier.scopusauthoridSun, H=7404827446en_US
dc.identifier.citeulike5343190-

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