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Article: Effects of charged amino-acid mutation on the solution structure of cytochrome b 5 and binding between cytochrome b 5 and cytochrome c

TitleEffects of charged amino-acid mutation on the solution structure of cytochrome b 5 and binding between cytochrome b 5 and cytochrome c
Authors
KeywordsSpecies Index: Bovinae
Issue Date2001
PublisherWiley-Blackwell Publishing, Inc.. The Journal's web site is located at http://www.proteinscience.org
Citation
Protein Science, 2001, v. 10 n. 12, p. 2451-2459 How to Cite?
AbstractThe solution structure of oxidized bovine microsomal cytochrome b 5 mutant (E48, E56/A, D60/A) has been determined through 1524 meaningful nuclear Overhauser effect constraints together with 190 pseudocontact shift constraints. The final family of 35 conformers has rmsd values with respect to the mean structure of 0.045±0.009 nm and 0.088±0.011 nm for backbone and heavy atoms, respectively. A characteristic of this mutant is that of having no significant changes in the whole folding and secondary structure compared with the X-ray and solution structures of wild-type cytochrome b 5. The binding of different surface mutants of cytochrome b 5 with cytochrome c shows that electrostatic interactions play an important role in maintaining the stability and specificity of the protein complex formed. The differences in association constants demonstrate the electrostatic contributions of cytochrome b5 surface negatively charged residues, which were suggested to be involved in complex formation in the Northrup and Salemme models, have cumulative effect on the stability of cyt c-cyt b 5 complex, and the contribution of Glu48 is a little higher than that of Glu44. Moreover, our result suggests that the docking geometry proposed by Northrup, which is involved in the participation of Glu48, Glu56, Asp60, and heme propionate of cytochrome b 5, do occur in the association between cytochrome b 5 and cytochrome c.
Persistent Identifierhttp://hdl.handle.net/10722/91182
ISSN
2015 Impact Factor: 3.039
2015 SCImago Journal Rankings: 2.029
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorQian, Cen_HK
dc.contributor.authorYao, Yen_HK
dc.contributor.authorYe, Ken_HK
dc.contributor.authorWang, Jen_HK
dc.contributor.authorTang, Wen_HK
dc.contributor.authorWang, Yen_HK
dc.contributor.authorWang, Wen_HK
dc.contributor.authorLu, Jen_HK
dc.contributor.authorXie, Yen_HK
dc.contributor.authorHuang, Zen_HK
dc.date.accessioned2010-09-17T10:14:21Z-
dc.date.available2010-09-17T10:14:21Z-
dc.date.issued2001en_HK
dc.identifier.citationProtein Science, 2001, v. 10 n. 12, p. 2451-2459en_HK
dc.identifier.issn0961-8368en_HK
dc.identifier.urihttp://hdl.handle.net/10722/91182-
dc.description.abstractThe solution structure of oxidized bovine microsomal cytochrome b 5 mutant (E48, E56/A, D60/A) has been determined through 1524 meaningful nuclear Overhauser effect constraints together with 190 pseudocontact shift constraints. The final family of 35 conformers has rmsd values with respect to the mean structure of 0.045±0.009 nm and 0.088±0.011 nm for backbone and heavy atoms, respectively. A characteristic of this mutant is that of having no significant changes in the whole folding and secondary structure compared with the X-ray and solution structures of wild-type cytochrome b 5. The binding of different surface mutants of cytochrome b 5 with cytochrome c shows that electrostatic interactions play an important role in maintaining the stability and specificity of the protein complex formed. The differences in association constants demonstrate the electrostatic contributions of cytochrome b5 surface negatively charged residues, which were suggested to be involved in complex formation in the Northrup and Salemme models, have cumulative effect on the stability of cyt c-cyt b 5 complex, and the contribution of Glu48 is a little higher than that of Glu44. Moreover, our result suggests that the docking geometry proposed by Northrup, which is involved in the participation of Glu48, Glu56, Asp60, and heme propionate of cytochrome b 5, do occur in the association between cytochrome b 5 and cytochrome c.en_HK
dc.languageengen_HK
dc.publisherWiley-Blackwell Publishing, Inc.. The Journal's web site is located at http://www.proteinscience.orgen_HK
dc.relation.ispartofProtein Scienceen_HK
dc.subjectSpecies Index: Bovinaeen_HK
dc.subject.meshAmino Acid Sequenceen_HK
dc.subject.meshAnimalsen_HK
dc.subject.meshAspartic Acid - chemistryen_HK
dc.subject.meshCattleen_HK
dc.subject.meshCrystallography, X-Rayen_HK
dc.subject.meshCytochrome c Group - chemistry - metabolismen_HK
dc.subject.meshCytochromes b5 - chemistry - genetics - metabolismen_HK
dc.subject.meshDose-Response Relationship, Drugen_HK
dc.subject.meshGlutamic Acid - chemistryen_HK
dc.subject.meshHorsesen_HK
dc.subject.meshHydrogen-Ion Concentrationen_HK
dc.subject.meshLiver - metabolismen_HK
dc.subject.meshMagnetic Resonance Spectroscopyen_HK
dc.subject.meshModels, Molecularen_HK
dc.subject.meshMolecular Sequence Dataen_HK
dc.subject.meshMutationen_HK
dc.subject.meshMyocardium - metabolismen_HK
dc.subject.meshProtein Bindingen_HK
dc.subject.meshProtein Conformationen_HK
dc.subject.meshProtein Foldingen_HK
dc.subject.meshProtein Structure, Secondaryen_HK
dc.subject.meshSequence Homology, Amino Aciden_HK
dc.titleEffects of charged amino-acid mutation on the solution structure of cytochrome b 5 and binding between cytochrome b 5 and cytochrome cen_HK
dc.typeArticleen_HK
dc.identifier.emailQian, C:cmqian@hku.hken_HK
dc.identifier.authorityQian, C=rp01371en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1110/ps.ps.12401en_HK
dc.identifier.pmid11714912-
dc.identifier.scopuseid_2-s2.0-0035182942en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0035182942&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume10en_HK
dc.identifier.issue12en_HK
dc.identifier.spage2451en_HK
dc.identifier.epage2459en_HK
dc.identifier.isiWOS:000172416600004-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridQian, C=7202311105en_HK
dc.identifier.scopusauthoridYao, Y=55202633100en_HK
dc.identifier.scopusauthoridYe, K=22942540900en_HK
dc.identifier.scopusauthoridWang, J=7701336117en_HK
dc.identifier.scopusauthoridTang, W=7403430524en_HK
dc.identifier.scopusauthoridWang, Y=8513746300en_HK
dc.identifier.scopusauthoridWang, W=7501757664en_HK
dc.identifier.scopusauthoridLu, J=26662977000en_HK
dc.identifier.scopusauthoridXie, Y=7403958906en_HK
dc.identifier.scopusauthoridHuang, Z=7406221847en_HK

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