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Article: The N-terminal domain of the Caulobacter crescentus CgtA protein does not function as a guanine nucleotide exchange factor

TitleThe N-terminal domain of the Caulobacter crescentus CgtA protein does not function as a guanine nucleotide exchange factor
Authors
KeywordsChemicals And Cas Registry Numbers
Issue Date2000
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/febslet
Citation
FEBS Letters, 2000, v. 484 n. 1, p. 29-32 How to Cite?
AbstractThe Caulobacter crescentus GTP binding protein CgtA is a member of the Obg/GTP1 subfamily of monomeric GTP binding proteins. In vitro, CgtA displays moderate affinity for both GDP and GTP, and rapid exchange rate constants for either nucleotide. One possible explanation for the observed rapid guanine nucleotide exchange factor (GEF) rates is that CgtA is a bimodal protein with a C-terminal GTP binding domain and an N-terminal GEF domain. In this study we demonstrate that although the N-terminus of CgtA is required for function in vivo, this domain plays no significant role in the guanine nucleotide binding, exchange or GTPase activity. (C) 2000 Federation of European Biochemical Societies.
Persistent Identifierhttp://hdl.handle.net/10722/90890
ISSN
2015 Impact Factor: 3.519
2015 SCImago Journal Rankings: 2.026
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLin, Ben_HK
dc.contributor.authorMaddock, JRen_HK
dc.date.accessioned2010-09-17T10:09:55Z-
dc.date.available2010-09-17T10:09:55Z-
dc.date.issued2000en_HK
dc.identifier.citationFEBS Letters, 2000, v. 484 n. 1, p. 29-32en_HK
dc.identifier.issn0014-5793en_HK
dc.identifier.urihttp://hdl.handle.net/10722/90890-
dc.description.abstractThe Caulobacter crescentus GTP binding protein CgtA is a member of the Obg/GTP1 subfamily of monomeric GTP binding proteins. In vitro, CgtA displays moderate affinity for both GDP and GTP, and rapid exchange rate constants for either nucleotide. One possible explanation for the observed rapid guanine nucleotide exchange factor (GEF) rates is that CgtA is a bimodal protein with a C-terminal GTP binding domain and an N-terminal GEF domain. In this study we demonstrate that although the N-terminus of CgtA is required for function in vivo, this domain plays no significant role in the guanine nucleotide binding, exchange or GTPase activity. (C) 2000 Federation of European Biochemical Societies.en_HK
dc.languageengen_HK
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/febsleten_HK
dc.relation.ispartofFEBS Lettersen_HK
dc.subjectChemicals And Cas Registry Numbersen_HK
dc.titleThe N-terminal domain of the Caulobacter crescentus CgtA protein does not function as a guanine nucleotide exchange factoren_HK
dc.typeArticleen_HK
dc.identifier.emailLin, B:blin@hku.hken_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/S0014-5793(00)02121-9en_HK
dc.identifier.pmid11056216-
dc.identifier.scopuseid_2-s2.0-0034721741en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0034721741&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume484en_HK
dc.identifier.issue1en_HK
dc.identifier.spage29en_HK
dc.identifier.epage32en_HK
dc.identifier.isiWOS:000165142700006-

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