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Crystal structure of Rnd3/RhoE: functional implications 1
Author(s) -
Fiegen Dennis,
Blumenstein Lars,
Stege Patricia,
Vetter Ingrid R,
Ahmadian Mohammad Reza
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03094-6
Subject(s) - gtpase , rhoa , subfamily , crystal structure , chemistry , transferase , gtp' , crystallography , amino acid , effector , stereochemistry , biology , biochemistry , enzyme , signal transduction , gene
The Rnd proteins constitute an exceptional subfamily within the Rho GTPase family. They possess extended chains at both termini and four prominent amino acid deviations causing GTPase deficiency. Herein, we report the crystal structure of the Rnd3/RhoE G‐domain (amino acids 19–200) at 2.0 Å resolution. This is the first GTP‐structure of a Rho family member which reveals a similar fold but striking differences from RhoA concerning (i) GTPase center, (ii) charge distribution at several surface areas, (iii) C3‐transferase binding site and (iv) interacting interfaces towards RhoA regulators and effectors.