1z2x
From Proteopedia
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| - | [[Image:1z2x.gif|left|200px]] | + | [[Image:1z2x.gif|left|200px]] |
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| - | '''Crystal structure of mouse Vps29''' | + | {{Structure |
| + | |PDB= 1z2x |SIZE=350|CAPTION= <scene name='initialview01'>1z2x</scene>, resolution 2.22Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= Vps29 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of mouse Vps29''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1Z2X is a [ | + | 1Z2X is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z2X OCA]. |
==Reference== | ==Reference== | ||
| - | Vps29 has a phosphoesterase fold that acts as a protein interaction scaffold for retromer assembly., Collins BM, Skinner CF, Watson PJ, Seaman MN, Owen DJ, Nat Struct Mol Biol. 2005 Jul;12(7):594-602. Epub 2005 Jun 19. PMID:[http:// | + | Vps29 has a phosphoesterase fold that acts as a protein interaction scaffold for retromer assembly., Collins BM, Skinner CF, Watson PJ, Seaman MN, Owen DJ, Nat Struct Mol Biol. 2005 Jul;12(7):594-602. Epub 2005 Jun 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15965486 15965486] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: vps29]] | [[Category: vps29]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:30:37 2008'' |
Revision as of 13:30, 20 March 2008
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| , resolution 2.22Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | Vps29 (Mus musculus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of mouse Vps29
Overview
The retromer complex is responsible for the retrieval of mannose 6-phosphate receptors from the endosomal system to the Golgi. Here we present the crystal structure of the mammalian retromer subunit mVps29 and show that it has structural similarity to divalent metal-containing phosphoesterases. mVps29 can coordinate metals in a similar manner but has no detectable phosphoesterase activity in vitro, suggesting a unique specificity or function. The mVps29 and mVps26 subunits bind independently to mVps35 and together form a high-affinity heterotrimeric subcomplex. Mutagenesis reveals the structural basis for the interaction of mVps29 with mVps35 and subsequent association with endosomal membranes in vivo. A conserved hydrophobic surface distinct from the primary Vps35p binding site mediates assembly of the Vps29p-Vps26p-Vps35p subcomplex with sorting nexins in yeast, and mutation of either site results in a defect in retromer-dependent membrane trafficking.
About this Structure
1Z2X is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Vps29 has a phosphoesterase fold that acts as a protein interaction scaffold for retromer assembly., Collins BM, Skinner CF, Watson PJ, Seaman MN, Owen DJ, Nat Struct Mol Biol. 2005 Jul;12(7):594-602. Epub 2005 Jun 19. PMID:15965486
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