1z2x: Difference between revisions

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[[Image:1z2x.gif|left|200px]]


{{Structure
==Crystal structure of mouse Vps29==
|PDB= 1z2x |SIZE=350|CAPTION= <scene name='initialview01'>1z2x</scene>, resolution 2.22&Aring;
<StructureSection load='1z2x' size='340' side='right'caption='[[1z2x]], [[Resolution|resolution]] 2.22&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[1z2x]] is a 2 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z2X FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.22&#8491;</td></tr>
|GENE= Vps29 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1z2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z2x OCA], [https://pdbe.org/1z2x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z2x RCSB], [https://www.ebi.ac.uk/pdbsum/1z2x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z2x ProSAT]</span></td></tr>
|DOMAIN=
</table>
|RELATEDENTRY=[[1s3m|1S3M]], [[1s3n|1S3N]], [[1z2w|1Z2W]]
== Function ==
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1z2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z2x OCA], [http://www.ebi.ac.uk/pdbsum/1z2x PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1z2x RCSB]</span>
[https://www.uniprot.org/uniprot/VPS29_MOUSE VPS29_MOUSE] Essential component of the retromer complex, a complex required to retrieve lysosomal enzyme receptors (IGF2R and M6PR) from endosomes to the trans-Golgi network. Also required to regulate transcytosis of the polymeric immunoglobulin receptor (pIgR-pIgA). Has low protein phosphatase activity towards a serine-phosphorylated peptide derived from IGF2R (in vitro) (By similarity). Has no activity towards p-nitrophenylphosphate, p-nitrophenylphosphorylcholine or phosphatidylinositlphosphates (in vitro).
}}
== Evolutionary Conservation ==
 
[[Image:Consurf_key_small.gif|200px|right]]
'''Crystal structure of mouse Vps29'''
Check<jmol>
 
  <jmolCheckbox>
 
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/z2/1z2x_consurf.spt"</scriptWhenChecked>
==Overview==
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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.
    <text>to colour the structure by Evolutionary Conservation</text>
 
  </jmolCheckbox>
==About this Structure==
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1z2x ConSurf].
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].  
<div style="clear:both"></div>
 
__TOC__
==Reference==
</StructureSection>
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: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Collins BM]]
[[Category: Collins, B M.]]
[[Category: Owen DJ]]
[[Category: Owen, D J.]]
[[Category: Seaman MNJ]]
[[Category: Seaman, M N.J.]]
[[Category: Skinner CF]]
[[Category: Skinner, C F.]]
[[Category: Watson PJ]]
[[Category: Watson, P J.]]
[[Category: phosphatase]]
[[Category: retromer]]
[[Category: vps29]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:28:18 2008''

Latest revision as of 16:38, 13 March 2024

Crystal structure of mouse Vps29Crystal structure of mouse Vps29

Structural highlights

1z2x is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.22Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

VPS29_MOUSE Essential component of the retromer complex, a complex required to retrieve lysosomal enzyme receptors (IGF2R and M6PR) from endosomes to the trans-Golgi network. Also required to regulate transcytosis of the polymeric immunoglobulin receptor (pIgR-pIgA). Has low protein phosphatase activity towards a serine-phosphorylated peptide derived from IGF2R (in vitro) (By similarity). Has no activity towards p-nitrophenylphosphate, p-nitrophenylphosphorylcholine or phosphatidylinositlphosphates (in vitro).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

1z2x, resolution 2.22Å

Drag the structure with the mouse to rotate

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