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1tq4

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(New page: 200px<br /><applet load="1tq4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tq4, resolution 1.95&Aring;" /> '''Crystal Structure of...)
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Revision as of 01:23, 21 November 2007

Image:1tq4.jpg

1tq4, resolution 1.95Å

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Crystal Structure of IIGP1: a paradigm for interferon inducible p47 resistance GTPases

Overview

Interferon-inducible p47 GTPases are critical mediators of cell-autonomous, resistance against several intracellular pathogens. Here we present the, first crystal structure of a member of this novel GTPase family, IIGP1, in, its nucleotide-free, GDP-, and GppNHp-bound form. The structure shows a, Ras-like G domain between an N-terminal three-helix bundle and a complex, system of C-terminal helices and loops. Sequence comparison and secondary, structure prediction suggest the IIGP1 structure to be a valid model for, the p47 GTPase family. The IIGP1 crystals contain a noncrystallographic, dimer. We show that the dimer is required for cooperative GTP hydrolysis, and GTP-dependent oligomerization of IIGP1. We also present the GDP- and, GppNHp-bound monomeric structures of two dimer interface mutants. Our, structures direct approaches to the analysis of the catalytic mechanism of, IIGP1 and provide a coherent basis for structure-function studies aimed at, elucidating the mechanistic basis of pathogen resistance caused by these, enigmatic GTPases.

About this Structure

1TQ4 is a Single protein structure of sequence from Mus musculus with MG and GDP as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of IIGP1: a paradigm for interferon-inducible p47 resistance GTPases., Ghosh A, Uthaiah R, Howard J, Herrmann C, Wolf E, Mol Cell. 2004 Sep 10;15(5):727-39. PMID:15350217

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