1TQD

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

Summary for 1TQD

• Entry DOI: 10.2210/pdb1tqd/pdb
• Related: 1DG3 1F5N 1TPZ 1TQ2 1TQ4 1TQ6
• Descriptor: interferon-inducible GTPase, SULFATE ION, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ... (4 entities in total)
• Functional Keywords: gtpase, interferon gamma, dimer, immunology, signaling protein
• Biological source: Mus musculus (house mouse)
• Cellular location: Cytoplasm: Q9QZ85
• Total number of polymer chains: 2
• Total formula weight: 95552.46

Authors

Ghosh, A.,Uthaiah, R.,Howard, J.,Herrmann, C.,Wolf, E. (deposition date: 2004-06-17, release date: 2004-09-21, Last modification date: 2024-03-13)

Primary citation

Ghosh, A.,Uthaiah, R.,Howard, J.,Herrmann, C.,Wolf, E.
Crystal Structure of IIGP1; A Paradigm for Interferon-Inducible p47 Resistance GTPases
Mol.Cell, 15:727-739, 2004

PubMed Abstract: 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.

PubMed: 15350217
DOI: 10.1016/j.molcel.2004.07.017

Experimental method

X-RAY DIFFRACTION (2.3 Å)