1TQ2
Crystal Structure of IIGP1: a paradigm for interferon inducible p47 resistance GTPases
Summary for 1TQ2
Entry DOI | 10.2210/pdb1tq2/pdb |
Related | 1DG3 1F5N 1TPZ 1TQ4 1TQ6 1TQD |
Descriptor | interferon-inducible GTPase, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, MAGNESIUM ION, ... (5 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 | 98632.61 |
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 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 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: 15350217DOI: 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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