1ocu: Difference between revisions

Revision as of 16:28, 5 November 2007

CRYSTAL STRUCTURE OF THE YEAST PX-DOMAIN PROTEIN GRD19P (SORTING NEXIN 3) COMPLEXED TO PHOSPHATIDYLINOSYTOL-3-PHOSPAHTE.

OverviewOverview

Phox homology (PX) domains have been recently identified in a number of, different proteins and are involved in various cellular functions such as, vacuolar targeting and membrane protein trafficking. It was shown that, these modules of about 130 amino acids specifically binding to, phosphoinositides and that this interaction is crucial for their cellular, function. The yeast genome contains 17 PX domain proteins. One of these, Grd19p, is involved in the localization of the late Golgi membrane, proteins DPAP A and Kex2p. Grd19p consists of the PX domain with 30 extra, residues at the N-terminal and is homologous to the functionally, characterized human sorting nexin protein SNX3. We determined the 2.0 A, crystal structure of Grd19p in the free form and in complex with, d-myo-phosphatidylinositol 3-phosphate (diC4PtdIns(3)P), representing the, first case of both free and ligand-bound conformations of the same PX, module. The ligand occupies a well defined positively charged binding, pocket at the interface between the beta-sheet and alpha-helical parts of, the molecule. The structure of the free and bound protein are globally, similar but show some significant differences in a region containing a, polyproline peptide and a putative membrane attachment site.

About this StructureAbout this Structure

1OCU is a Single protein structure of sequence from Saccharomyces cerevisiae with PIB as ligand. Structure known Active Site: AC1. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the yeast Phox homology (PX) domain protein Grd19p complexed to phosphatidylinositol-3-phosphate., Zhou CZ, de La Sierra-Gallay IL, Quevillon-Cheruel S, Collinet B, Minard P, Blondeau K, Henckes G, Aufrere R, Leulliot N, Graille M, Sorel I, Savarin P, de la Torre F, Poupon A, Janin J, van Tilbeurgh H, J Biol Chem. 2003 Dec 12;278(50):50371-6. Epub 2003 Sep 26. PMID:14514667

Page seeded by OCA on Mon Nov 5 15:33:48 2007

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OCA

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 ==Overview==
-Phox homology (PX) domains have been recently identified in a number of, different proteins and are involved in various cellular functions such as, vacuolar targeting and membrane protein trafficking. It was shown that, these modules of about 130 amino acids specifically binding to, phosphoinositides and that this interaction is crucial for their cellular, function. The yeast genome contains 17 PX domain proteins. One of these, Grd19p, is involved in the localization of the late Golgi membrane, proteins DPAP A and Kex2p. Grd19p consists of the PX domain with 30 extra, residues at the N-terminal and is homologous to the functionally, characterized human sorting nexin protein SNX3. We determined the 2.0 A, crystal structure of Grd19p in the free form and in complex with, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?14514667 (full description)]]
+Phox homology (PX) domains have been recently identified in a number of, different proteins and are involved in various cellular functions such as, vacuolar targeting and membrane protein trafficking. It was shown that, these modules of about 130 amino acids specifically binding to, phosphoinositides and that this interaction is crucial for their cellular, function. The yeast genome contains 17 PX domain proteins. One of these, Grd19p, is involved in the localization of the late Golgi membrane, proteins DPAP A and Kex2p. Grd19p consists of the PX domain with 30 extra, residues at the N-terminal and is homologous to the functionally, characterized human sorting nexin protein SNX3. We determined the 2.0 A, crystal structure of Grd19p in the free form and in complex with, d-myo-phosphatidylinositol 3-phosphate (diC4PtdIns(3)P), representing the, first case of both free and ligand-bound conformations of the same PX, module. The ligand occupies a well defined positively charged binding, pocket at the interface between the beta-sheet and alpha-helical parts of, the molecule. The structure of the free and bound protein are globally, similar but show some significant differences in a region containing a, polyproline peptide and a putative membrane attachment site.
 ==About this Structure==
-OCU is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]] with PIB as [[http://en.wikipedia.org/wiki/ligand ligand]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OCU OCA]].
+OCU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with PIB as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OCU OCA].
 ==Reference==
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 [[Category: yeast protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:49:55 2007''
+''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov  5 15:33:48 2007''