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Article: Preparation, crystallization and X-ray diffraction analysis to 1.5 Å resolution of rat cysteine dioxygenase, a mononuclear iron enzyme responsible for cysteine thiol oxidation

TitlePreparation, crystallization and X-ray diffraction analysis to 1.5 Å resolution of rat cysteine dioxygenase, a mononuclear iron enzyme responsible for cysteine thiol oxidation
Authors
Issue Date2005
PublisherWiley-Blackwell Publishing, Inc.. The Journal's web site is located at http://www3.interscience.wiley.com/journal/117982340/home
Citation
Acta Crystallographica Section F: Structural Biology And Crystallization Communications, 2005, v. 61 n. 11, p. 1013-1016 How to Cite?
AbstractCysteine dioxygenase (CDO; EC 1.13.11.20) is an ∼23 kDa non-heme iron metalloenzyme that is responsible for the oxidation of cysteine by O 2, yielding cysteinesulfinate. CDO catalyzes the first step in the conversion of cysteine to taurine, as well as the first step in the catabolism of cysteine to pyruvate plus sulfate. Recombinant rat CDO was heterologously expressed, purified and crystallized. The protein was expressed as a fusion protein bearing a polyhistidine tag to facilitate purification, a thioredoxin tag to improve solubility and a factor Xa cleavage site to permit removal of the entire N-terminus, leaving only the 200 amino acids inherent to the native protein. A multi-step purification scheme was used to achieve >95% purity of CDO. The optimal CDO crystals diffracted to 1.5 Å resolution and belonged to space group P43212 or P41212, with unit-cell parameters a = b = 57.55, c = 123.06 Å, α = β = γ = 90°. CDO shows little homology to any other proteins; therefore, the structure of the enzyme will be determined by ab initio phasing using a selenomethionyl derivative. © 2005 International Union of Crystallography All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/91936
ISSN
2014 Impact Factor: 0.524
PubMed Central ID
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorSimmons, CRen_HK
dc.contributor.authorHao, Qen_HK
dc.contributor.authorStipanuk, MHen_HK
dc.date.accessioned2010-09-17T10:31:02Z-
dc.date.available2010-09-17T10:31:02Z-
dc.date.issued2005en_HK
dc.identifier.citationActa Crystallographica Section F: Structural Biology And Crystallization Communications, 2005, v. 61 n. 11, p. 1013-1016en_HK
dc.identifier.issn1744-3091en_HK
dc.identifier.urihttp://hdl.handle.net/10722/91936-
dc.description.abstractCysteine dioxygenase (CDO; EC 1.13.11.20) is an ∼23 kDa non-heme iron metalloenzyme that is responsible for the oxidation of cysteine by O 2, yielding cysteinesulfinate. CDO catalyzes the first step in the conversion of cysteine to taurine, as well as the first step in the catabolism of cysteine to pyruvate plus sulfate. Recombinant rat CDO was heterologously expressed, purified and crystallized. The protein was expressed as a fusion protein bearing a polyhistidine tag to facilitate purification, a thioredoxin tag to improve solubility and a factor Xa cleavage site to permit removal of the entire N-terminus, leaving only the 200 amino acids inherent to the native protein. A multi-step purification scheme was used to achieve >95% purity of CDO. The optimal CDO crystals diffracted to 1.5 Å resolution and belonged to space group P43212 or P41212, with unit-cell parameters a = b = 57.55, c = 123.06 Å, α = β = γ = 90°. CDO shows little homology to any other proteins; therefore, the structure of the enzyme will be determined by ab initio phasing using a selenomethionyl derivative. © 2005 International Union of Crystallography All rights reserved.en_HK
dc.languageengen_HK
dc.publisherWiley-Blackwell Publishing, Inc.. The Journal's web site is located at http://www3.interscience.wiley.com/journal/117982340/homeen_HK
dc.relation.ispartofActa Crystallographica Section F: Structural Biology and Crystallization Communicationsen_HK
dc.titlePreparation, crystallization and X-ray diffraction analysis to 1.5 Å resolution of rat cysteine dioxygenase, a mononuclear iron enzyme responsible for cysteine thiol oxidationen_HK
dc.typeArticleen_HK
dc.identifier.emailHao, Q: qhao@hku.hken_HK
dc.identifier.authorityHao, Q=rp01332en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1107/S1744309105033737en_HK
dc.identifier.pmid16511222en_HK
dc.identifier.pmcidPMC1978133-
dc.identifier.scopuseid_2-s2.0-33744475636en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-33744475636&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume61en_HK
dc.identifier.issue11en_HK
dc.identifier.spage1013en_HK
dc.identifier.epage1016en_HK
dc.identifier.isiWOS:000232890200016-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridSimmons, CR=13102585800en_HK
dc.identifier.scopusauthoridHao, Q=7102508868en_HK
dc.identifier.scopusauthoridStipanuk, MH=7004251179en_HK

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