1tq6

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(New page: 200px<br /><applet load="1tq6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tq6, resolution 2.7&Aring;" /> '''Crystal Structure of ...)
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caption="1tq6, resolution 2.7&Aring;" />
'''Crystal Structure of IIGP1: a paradigm for interferon inducible p47 resistance GTPases'''<br />
'''Crystal Structure of IIGP1: a paradigm for interferon inducible p47 resistance GTPases'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1TQ6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with MG and GNP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TQ6 OCA].
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1TQ6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=GNP:'>GNP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TQ6 OCA].
==Reference==
==Reference==
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[[Category: interferon gamma]]
[[Category: interferon gamma]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:30:26 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:16:11 2008''

Revision as of 13:16, 21 February 2008


1tq6, resolution 2.7Å

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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

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