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Article: Assembly of preactivation complex for urease maturation in Helicobacter pylori: crystal structure of UreF-UreH protein complex

TitleAssembly of preactivation complex for urease maturation in Helicobacter pylori: crystal structure of UreF-UreH protein complex
Authors
Issue Date2011
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
Citation
Journal of Biological Chemistry, 2011, v. 286 n. 50, p. 43241-43249 How to Cite?
AbstractColonization of Helicobacter pylori in the acidic environment of the human stomach depends on the neutralizing activity of urease. Activation of apo-urease involves carboxylation of lysine 219 and insertion of two nickel ions. In H. pylori, this maturation process involves four urease accessory proteins as follows: UreE, UreF, UreG, and UreH. It is postulated that the apo-urease interacts with UreF, UreG, and UreH to form a pre-activation complex that undergoes GTP-dependent activation of urease. The crystal structure of the UreF-UreH complex reveals conformational changes in two distinct regions of UreF upon complex formation. First, the flexible C-terminal residues of UreF become ordered, forming an extra helix alpha10 and a loop structure stabilized by hydrogen bonds involving Arg-250. Second, the first turn of helix alpha2 uncoils to expose a conserved residue, Tyr-48. Substitution of R250A or Y48A in UreF abolishes the formation of the heterotrimeric complex of UreG-UreF-UreH and abolishes urease maturation. Our results suggest that the C-terminal residues and helix alpha2 of UreF are essential for the recruitment of UreG for the formation of the pre-activation complex. The molecular mass of the UreF-UreH complex determined by static light scattering was 116 +/- 2.3 kDa, which is consistent with the quaternary structure of a dimer of heterodimers observed in the crystal structure. Taking advantage of the unique 2-fold symmetry observed in both the crystal structures of H. pylori urease and the UreF-UreH complex, we proposed a topology model of the pre-activation complex for urease maturation.
Persistent Identifierhttp://hdl.handle.net/10722/159373
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
PubMed Central ID
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorFong, YHen_US
dc.contributor.authorWong, HCen_US
dc.contributor.authorChuck, CPen_US
dc.contributor.authorChen, YWen_US
dc.contributor.authorSun, Hen_US
dc.contributor.authorWong, KBen_US
dc.date.accessioned2012-08-16T05:48:55Z-
dc.date.available2012-08-16T05:48:55Z-
dc.date.issued2011en_US
dc.identifier.citationJournal of Biological Chemistry, 2011, v. 286 n. 50, p. 43241-43249en_US
dc.identifier.issn0021-9258en_US
dc.identifier.urihttp://hdl.handle.net/10722/159373-
dc.description.abstractColonization of Helicobacter pylori in the acidic environment of the human stomach depends on the neutralizing activity of urease. Activation of apo-urease involves carboxylation of lysine 219 and insertion of two nickel ions. In H. pylori, this maturation process involves four urease accessory proteins as follows: UreE, UreF, UreG, and UreH. It is postulated that the apo-urease interacts with UreF, UreG, and UreH to form a pre-activation complex that undergoes GTP-dependent activation of urease. The crystal structure of the UreF-UreH complex reveals conformational changes in two distinct regions of UreF upon complex formation. First, the flexible C-terminal residues of UreF become ordered, forming an extra helix alpha10 and a loop structure stabilized by hydrogen bonds involving Arg-250. Second, the first turn of helix alpha2 uncoils to expose a conserved residue, Tyr-48. Substitution of R250A or Y48A in UreF abolishes the formation of the heterotrimeric complex of UreG-UreF-UreH and abolishes urease maturation. Our results suggest that the C-terminal residues and helix alpha2 of UreF are essential for the recruitment of UreG for the formation of the pre-activation complex. The molecular mass of the UreF-UreH complex determined by static light scattering was 116 +/- 2.3 kDa, which is consistent with the quaternary structure of a dimer of heterodimers observed in the crystal structure. Taking advantage of the unique 2-fold symmetry observed in both the crystal structures of H. pylori urease and the UreF-UreH complex, we proposed a topology model of the pre-activation complex for urease maturation.-
dc.languageengen_US
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/en_US
dc.relation.ispartofJournal of Biological Chemistryen_US
dc.rightsJournal of Biological Chemistry. Copyright © American Society for Biochemistry and Molecular Biology, Inc.en_US
dc.subject.meshBacterial Proteins - chemistry - genetics - metabolism-
dc.subject.meshCarrier Proteins - chemistry - genetics - metabolism-
dc.subject.meshCrystallography, X-Ray - methods-
dc.subject.meshHelicobacter pylori - genetics - metabolism-
dc.subject.meshUrease - chemistry - genetics - metabolism-
dc.titleAssembly of preactivation complex for urease maturation in Helicobacter pylori: crystal structure of UreF-UreH protein complexen_US
dc.typeArticleen_US
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0021-9258&volume=286&spage=43241&epage=43249&date=2011&atitle=Assembly+of+the+preactivation+complex+for+urease+maturation+in+Helicobacter+pylori:+crystal+structure+of+the+UreF/UreH+complexen_US
dc.identifier.emailWong, HC: kbwong@cuhk.edu.hken_US
dc.identifier.emailSun, H: hsun@hku.hk-
dc.identifier.authoritySun, H=rp00777en_US
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1074/jbc.M111.296830-
dc.identifier.pmid22013070-
dc.identifier.pmcidPMC3234868-
dc.identifier.scopuseid_2-s2.0-83355169697-
dc.identifier.hkuros205067en_US
dc.identifier.volume286en_US
dc.identifier.issue50-
dc.identifier.spage43241en_US
dc.identifier.epage43249en_US
dc.identifier.isiWOS:000298351300044-
dc.publisher.placeUnited States-

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