1tq6
From Proteopedia
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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
1TQ6 is a Single protein structure of sequence from Mus musculus with and 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
Page seeded by OCA on Thu Feb 21 15:16:11 2008
Categories: Mus musculus | Single protein | Ghosh, A. | Herrmann, C. | Howard, J. | Uthaiah, R. | Wolf, E. | GNP | MG | Crystal structure | Dimer | Gtpase | Immunology | Interferon gamma
