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Article: 1H, 15N and 13C NMR resonance assignment, secondary structure and global fold of the FMN-binding domain of human cytochrome P450 reductase

Title1H, 15N and 13C NMR resonance assignment, secondary structure and global fold of the FMN-binding domain of human cytochrome P450 reductase
Authors
Issue Date1997
PublisherSpringer Verlag Dordrecht. The Journal's web site is located at http://springerlink.metapress.com/openurl.asp?genre=journal&issn=0925-2738
Citation
Journal Of Biomolecular Nmr, 1997, v. 10 n. 1, p. 63-75 How to Cite?
AbstractThe FMN-binding domain of human NADPH-cytochrome P450 reductase, corresponding to exons 3-7, has been expressed at high level in an active form and labelled with 13C and 15N. Most of the backbone and aliphatic side-chain 1H, 15N and 13C resonances have been assigned using heteronuclear double- and triple-resonance methods, together with a semiautomatic assignment strategy. The secondary structure as estimated from the chemical shift index and NOE connectivities consists of six α-helices and five β-strands. The global fold was deduced from the long-range NOEs unambiguously assigned in a 4D 13C-resolved HMQC-NOESY-HMQC spectrum. The fold is of the alternating α/β type, with the five β-strands arranged into a parallel β-sheet. The secondary structure and global fold are very similar to those of the bacterial flavodoxins, but the FMN-binding domain has an extra short helix in place of a loop, and an extra helix at the N-terminus (leading to the membrane anchor domain in the intact P450 reductase). The experimental constraints were combined with homology modelling to obtain a structure of the FMN-binding domain satisfying the observed NOE constraints. Chemical shift comparisons showed that the effects of FMN binding and of FMN reduction are largely localised at the binding site.
Persistent Identifierhttp://hdl.handle.net/10722/157279
ISSN
2015 Impact Factor: 3.439
2015 SCImago Journal Rankings: 2.043
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorBarsukov, Ien_US
dc.contributor.authorModi, Sen_US
dc.contributor.authorLian, LYen_US
dc.contributor.authorSze, KHen_US
dc.contributor.authorPaine, MJIen_US
dc.contributor.authorWolf, CRen_US
dc.contributor.authorRoberts, GCKen_US
dc.date.accessioned2012-08-08T08:48:36Z-
dc.date.available2012-08-08T08:48:36Z-
dc.date.issued1997en_US
dc.identifier.citationJournal Of Biomolecular Nmr, 1997, v. 10 n. 1, p. 63-75en_US
dc.identifier.issn0925-2738en_US
dc.identifier.urihttp://hdl.handle.net/10722/157279-
dc.description.abstractThe FMN-binding domain of human NADPH-cytochrome P450 reductase, corresponding to exons 3-7, has been expressed at high level in an active form and labelled with 13C and 15N. Most of the backbone and aliphatic side-chain 1H, 15N and 13C resonances have been assigned using heteronuclear double- and triple-resonance methods, together with a semiautomatic assignment strategy. The secondary structure as estimated from the chemical shift index and NOE connectivities consists of six α-helices and five β-strands. The global fold was deduced from the long-range NOEs unambiguously assigned in a 4D 13C-resolved HMQC-NOESY-HMQC spectrum. The fold is of the alternating α/β type, with the five β-strands arranged into a parallel β-sheet. The secondary structure and global fold are very similar to those of the bacterial flavodoxins, but the FMN-binding domain has an extra short helix in place of a loop, and an extra helix at the N-terminus (leading to the membrane anchor domain in the intact P450 reductase). The experimental constraints were combined with homology modelling to obtain a structure of the FMN-binding domain satisfying the observed NOE constraints. Chemical shift comparisons showed that the effects of FMN binding and of FMN reduction are largely localised at the binding site.en_US
dc.languageengen_US
dc.publisherSpringer Verlag Dordrecht. The Journal's web site is located at http://springerlink.metapress.com/openurl.asp?genre=journal&issn=0925-2738en_US
dc.relation.ispartofJournal of Biomolecular NMRen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshBinding Sitesen_US
dc.subject.meshCarbon Radioisotopesen_US
dc.subject.meshComputer Simulationen_US
dc.subject.meshFlavin Mononucleotide - Metabolismen_US
dc.subject.meshHumansen_US
dc.subject.meshHydrogenen_US
dc.subject.meshModels, Molecularen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshNadph-Ferrihemoprotein Reductase - Chemistry - Isolation & Purification - Metabolismen_US
dc.subject.meshNitrogen Isotopesen_US
dc.subject.meshNuclear Magnetic Resonance, Biomolecular - Methodsen_US
dc.subject.meshProtein Foldingen_US
dc.subject.meshProtein Structure, Secondaryen_US
dc.subject.meshRecombinant Proteins - Chemistry - Isolation & Purification - Metabolismen_US
dc.subject.meshSkin - Enzymologyen_US
dc.title1H, 15N and 13C NMR resonance assignment, secondary structure and global fold of the FMN-binding domain of human cytochrome P450 reductaseen_US
dc.typeArticleen_US
dc.identifier.emailSze, KH:khsze@hku.hken_US
dc.identifier.authoritySze, KH=rp00785en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.pmid9335117en_US
dc.identifier.scopuseid_2-s2.0-0031173906en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0031173906&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume10en_US
dc.identifier.issue1en_US
dc.identifier.spage63en_US
dc.identifier.epage75en_US
dc.identifier.isiWOS:A1997XX15600007-
dc.publisher.placeNetherlandsen_US
dc.identifier.scopusauthoridBarsukov, I=35586964900en_US
dc.identifier.scopusauthoridModi, S=7005772422en_US
dc.identifier.scopusauthoridLian, LY=7005156195en_US
dc.identifier.scopusauthoridSze, KH=7006735061en_US
dc.identifier.scopusauthoridPaine, MJI=7005943158en_US
dc.identifier.scopusauthoridWolf, CR=35451954100en_US
dc.identifier.scopusauthoridRoberts, GCK=7403400348en_US

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