File Download
There are no files associated with this item.
Links for fulltext
(May Require Subscription)
- Publisher Website: 10.1107/S1744309105033737
- Scopus: eid_2-s2.0-33744475636
- PMID: 16511222
- WOS: WOS:000232890200016
- Find via
Supplementary
- Citations:
- Appears in Collections:
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
Title | 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 |
---|---|
Authors | |
Issue Date | 2005 |
Publisher | Wiley-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? |
Abstract | Cysteine 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 Identifier | http://hdl.handle.net/10722/91936 |
ISSN | 2014 Impact Factor: 0.524 |
PubMed Central ID | |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Simmons, CR | en_HK |
dc.contributor.author | Hao, Q | en_HK |
dc.contributor.author | Stipanuk, MH | en_HK |
dc.date.accessioned | 2010-09-17T10:31:02Z | - |
dc.date.available | 2010-09-17T10:31:02Z | - |
dc.date.issued | 2005 | en_HK |
dc.identifier.citation | Acta Crystallographica Section F: Structural Biology And Crystallization Communications, 2005, v. 61 n. 11, p. 1013-1016 | en_HK |
dc.identifier.issn | 1744-3091 | en_HK |
dc.identifier.uri | http://hdl.handle.net/10722/91936 | - |
dc.description.abstract | Cysteine 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.language | eng | en_HK |
dc.publisher | Wiley-Blackwell Publishing, Inc.. The Journal's web site is located at http://www3.interscience.wiley.com/journal/117982340/home | en_HK |
dc.relation.ispartof | Acta Crystallographica Section F: Structural Biology and Crystallization Communications | en_HK |
dc.title | 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 | en_HK |
dc.type | Article | en_HK |
dc.identifier.email | Hao, Q: qhao@hku.hk | en_HK |
dc.identifier.authority | Hao, Q=rp01332 | en_HK |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.doi | 10.1107/S1744309105033737 | en_HK |
dc.identifier.pmid | 16511222 | en_HK |
dc.identifier.pmcid | PMC1978133 | - |
dc.identifier.scopus | eid_2-s2.0-33744475636 | en_HK |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-33744475636&selection=ref&src=s&origin=recordpage | en_HK |
dc.identifier.volume | 61 | en_HK |
dc.identifier.issue | 11 | en_HK |
dc.identifier.spage | 1013 | en_HK |
dc.identifier.epage | 1016 | en_HK |
dc.identifier.isi | WOS:000232890200016 | - |
dc.publisher.place | United States | en_HK |
dc.identifier.scopusauthorid | Simmons, CR=13102585800 | en_HK |
dc.identifier.scopusauthorid | Hao, Q=7102508868 | en_HK |
dc.identifier.scopusauthorid | Stipanuk, MH=7004251179 | en_HK |
dc.identifier.issnl | 1744-3091 | - |