File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

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 Date2001
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/febslet
Citation
FEBS Letters, 2001, v. 489 n. 1, p. 108-111 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 rates is that CgtA is a bimodal protein with a C-terminal GTP binding domain and an N-terminal guanine nucleotide exchange factor (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.
Persistent Identifierhttp://hdl.handle.net/10722/90921
ISSN
2015 Impact Factor: 3.519
2015 SCImago Journal Rankings: 2.026

 

DC FieldValueLanguage
dc.contributor.authorLin, Ben_HK
dc.contributor.authorMaddock, JRen_HK
dc.date.accessioned2010-09-17T10:10:23Z-
dc.date.available2010-09-17T10:10:23Z-
dc.date.issued2001en_HK
dc.identifier.citationFEBS Letters, 2001, v. 489 n. 1, p. 108-111en_HK
dc.identifier.issn0014-5793en_HK
dc.identifier.urihttp://hdl.handle.net/10722/90921-
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 rates is that CgtA is a bimodal protein with a C-terminal GTP binding domain and an N-terminal guanine nucleotide exchange factor (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.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 factor.en_HK
dc.typeArticleen_HK
dc.identifier.emailLin, B:blin@hku.hken_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.pmid11231024-
dc.identifier.scopuseid_2-s2.0-0035951819en_HK
dc.identifier.volume489en_HK
dc.identifier.issue1en_HK
dc.identifier.spage108en_HK
dc.identifier.epage111en_HK

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats