2p2l

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2p2l, resolution 1.90Å

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Rac1-GDP-Zinc Complex

Overview

The Rho family of small GTPases represent well characterized signaling, molecules that regulate many cellular functions such as actin cytoskeletal, arrangement and the cell cycle by acting as molecular switches. A, Rac1-GDP-Zn complex has been crystallized in space group P3(2)21 and its, crystal structure has been solved at 1.9 A resolution. These trigonal, crystals reveal the unexpected ability of Rac1 to coordinate Zn atoms in a, tetrahedral fashion by use of its biologically relevant switch I and, switch II regions. Upon coordination of zinc, the switch I region is, stabilized in the GDP-bound conformation and contributes to a Rac1 trimer, in the asymmetric unit. Zinc coordination causes switch II to adopt a, novel conformation with a symmetry-related molecule. Additionally, zinc, was found to displace magnesium from its octahedral coordination at switch, I, although GDP binding remained stable. This structure represents the, first reported Rac1-GDP-Zn complex, which further underscores the, conformational flexibility and versatility of the small GTPase switch, regions.

About this Structure

2P2L is a Single protein structure of sequence from Homo sapiens with ZN and GDP as ligands. Full crystallographic information is available from OCA.

Reference

A Rac1-GDP trimer complex binds zinc with tetrahedral and octahedral coordination, displacing magnesium., Prehna G, Stebbins CE, Acta Crystallogr D Biol Crystallogr. 2007 May;63(Pt 5):628-35. Epub 2007, Apr 21. PMID:17452788

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