1mr3

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Revision as of 19:31, 20 November 2007

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spinqualitylabelsall models 1mr3, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Saccharomyces cerevisiae ADP-ribosylation Factor 2 (ScArf2) complexed with GDP-3'P at 1.6A resolution

Overview

Structures were determined by x-ray crystallography for two members of the, ADP-ribosylation factor (ARF) family of regulatory GTPases, yeast ARF1 and, ARL1, and were compared with previously determined structures of human, ARF1 and ARF6. These analyses revealed an overall conserved fold but, differences in primary sequence and length, particularly in an N-terminal, loop, lead to differences in nucleotide and divalent metal binding., Packing of hydrophobic residues is central to the interplay between the, N-terminal alpha-helix, switch I, and the interswitch region, which along, with differences in surface electrostatics provide explanations for the, different biophysical and biochemical properties of ARF and ARF-like, proteins.

About this Structure

1MR3 is a Single protein structure of sequence from Saccharomyces cerevisiae with MG, G3D, EDO, GOL, EOH and PDO as ligands. Full crystallographic information is available from OCA.

Reference

Structures of yeast ARF2 and ARL1: distinct roles for the N terminus in the structure and function of ARF family GTPases., Amor JC, Horton JR, Zhu X, Wang Y, Sullards C, Ringe D, Cheng X, Kahn RA, J Biol Chem. 2001 Nov 9;276(45):42477-84. Epub 2001 Sep 4. PMID:11535602

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