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1TQ2

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

Summary for 1TQ2
Entry DOI10.2210/pdb1tq2/pdb
Related1DG3 1F5N 1TPZ 1TQ4 1TQ6 1TQD
Descriptorinterferon-inducible GTPase, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, MAGNESIUM ION, ... (5 entities in total)
Functional Keywordsgtpase, interferon gamma, dimer, immunology, signaling protein
Biological sourceMus musculus (house mouse)
Cellular locationCytoplasm: Q9QZ85
Total number of polymer chains2
Total formula weight98632.61
Authors
Ghosh, A.,Uthaiah, R.,Howard, J.,Herrmann, C.,Wolf, E. (deposition date: 2004-06-16, release date: 2004-09-21, Last modification date: 2024-03-13)
Primary citationGhosh, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.7 Å)
Structure validation

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