PDBsum entry 1m7b

Signaling protein

PDB id: 1m7b

Contents

Protein chain

179 a.a. *

Ligands

GTP

Metals

_MG

Waters ×49

* Residue conservation analysis

PDB id:

1m7b

Name:

Signaling protein

Title:

Crystal structure of rnd3/rhoe: functional implications

Structure:

Rnd3/rhoe small gtp-binding protein. Chain: a. Fragment: rnd3(residues 19-200). Synonym: rho-related gtp-binding protein rhoe. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: rnd3 (amino acids 19-200). Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Biol. unit:

Tetramer (from PQS)

Resolution:

2.00Å R-factor: 0.201 R-free: 0.243

Authors:

D.Fiegen,L.Blumenstein,P.Stege,I.R.Vetter,M.R.Ahmadian

Key ref:

D.Fiegen et al. (2002). Crystal structure of Rnd3/RhoE: functional implications. FEBS Lett, 525, 100-104. PubMed id: 12163169 DOI: 10.1016/S0014-5793(02)03094-6

Date:

19-Jul-02 Release date: 07-Aug-02

Protein chain

P61587  (RND3_HUMAN) -  Rho-related GTP-binding protein RhoE from Homo sapiens

Seq: 244 a.a.

Struc: 179 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1016/S0014-5793(02)03094-6

FEBS Lett 525:100-104 (2002)

PubMed id: 12163169

Crystal structure of Rnd3/RhoE: functional implications.

D.Fiegen, L.Blumenstein, P.Stege, I.R.Vetter, M.R.Ahmadian.

ABSTRACT

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 A 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.

Selected figure(s)

Figure 1.
Fig. 1. Rnd3 Structure. Ribbon representation of Rnd3·GTP (green) compared with RhoA(G12V)·GTPγS (grey) [17] were analyzed by the program DSSP [40] and drawn using the program Bobscript [41 and 42]. Structural comparison of Rnd3 and RhoA was carried out with the least squares option of the program O [18]. P-loop, switch I, switch II and insert-helix are highlighted in orange.

Figure 3.
Fig. 3. Comparison of the surface and interacting areas of Rnd3 and RhoA. A: Surface deviations. Rnd3 (left panel) and RhoA (right panel) in the same orientation (upper panel) as in Fig. 1 and the back view (180° rotation around x-axis, lower panel) are presented as GRASP images [43]. Positively charged amino acids are blue, negatively charged amino acids are red. Surface residues deviating between Rnd3 and RhoA are marked (single letter code). B: Interacting interfaces of RhoA. Residues of RhoA involved in binding of RhoGDI (green), p50RhoGAP (blue), PKN (pink) and C3-transferases (orange) and the corresponding residues of Rnd3 are highlighted.

The above figures are reprinted by permission from the Federation of European Biochemical Societies: FEBS Lett (2002, 525, 100-104) copyright 2002.

Figures were selected by an automated process.