1Z2W

Crystal structure of mouse Vps29 complexed with Mn2+

Summary for 1Z2W

• Entry DOI: 10.2210/pdb1z2w/pdb
• Related: 1S3M 1S3N 1Z2X
• Descriptor: Vacuolar protein sorting 29, MANGANESE (II) ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: vps29, retromer, phosphatase, manganese, protein transport
• Biological source: Mus musculus (house mouse)
• Cellular location: Cytoplasm (By similarity): Q9QZ88
• Total number of polymer chains: 2
• Total formula weight: 43933.89

Authors

Collins, B.M.,Skinner, C.F.,Watson, P.J.,Seaman, M.N.J.,Owen, D.J. (deposition date: 2005-03-10, release date: 2005-06-21, Last modification date: 2023-10-25)

Primary citation

Collins, B.M.,Skinner, C.F.,Watson, P.J.,Seaman, M.N.J.,Owen, D.J.
Vps29 has a phosphoesterase fold that acts as a protein interaction scaffold for retromer assembly
NAT.STRUCT.MOL.BIOL., 12:594-602, 2005

PubMed Abstract: 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.

PubMed: 15965486
DOI: 10.1038/nsmb954

Experimental method

X-RAY DIFFRACTION (2 Å)