Please use this identifier to cite or link to this item: http://dl.umsu.ac.ir/handle/10722/90921
Title: The N-terminal domain of the Caulobacter crescentus CgtA protein does not function as a guanine nucleotide exchange factor.
Authors: Lin, B;Maddock, JR
subject: Chemicals And Cas Registry Numbers
Year: 2001
Publisher: Elsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/febslet
Description: The 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.
URI: http://hub.hku.hk/handle/10722/90921
Standard no: FEBS Letters, 2001, v. 489 n. 1, p. 108-111
111
0014-5793
1
11231024
eid_2-s2.0-0035951819
108
489
Appears in Collections:Department of Anatomy

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