3LH9

Crystal structure of mouse VPS26B(L197S/R199E) in spacegroup P41 21 2

Summary for 3LH9

• Entry DOI: 10.2210/pdb3lh9/pdb
• Related: 2FAU 2R51 3LH9 3LHA
• Descriptor: Vacuolar protein sorting-associated protein 26B (2 entities in total)
• Functional Keywords: arrestin, fibronectin, membrane, protein transport, transport
• Biological source: Mus musculus (mouse)
• Cellular location: Cytoplasm: Q8C0E2
• Total number of polymer chains: 2
• Total formula weight: 79297.95

Authors

Collins, B.,Shaw, D.,Norwood, S. (deposition date: 2010-01-21, release date: 2010-02-02, Last modification date: 2023-09-06)

Primary citation

Norwood, S.J.,Shaw, D.J.,Cowieson, N.P.,Owen, D.J.,Teasdale, R.D.,Collins, B.M.
Assembly and solution structure of the core retromer protein complex.
Traffic, 12:56-71, 2011

PubMed Abstract: Retromer is a peripheral membrane protein complex that has pleiotropic roles in endosomal membrane trafficking. The core of retromer possesses three subunits, VPS35, VPS29 and VPS26, that play different roles in binding to cargo, regulatory proteins and complex stabilization. We have performed an investigation of the thermodynamics of core retromer assembly using isothermal titration calorimetry (ITC) demonstrating that VPS35 acts as the central subunit to which VPS29 and VPS26 bind independently. Furthermore, we confirm that the conserved PRLYL motif of the large VPS35 subunit is critical for direct VPS26 interaction. Heat capacity measurements of VPS29 and VPS26 binding to VPS35 indicate extensive binding interfaces and suggest conformational alterations in VPS29 or VPS35 upon complex formation. Solution studies of the retromer core using small-angle X-ray scattering allow us to propose a model whereby VPS35 forms an extended platform with VPS29 and VPS26 bound at distal ends, with the potential for forming dimeric assemblies.

PubMed: 20875039
DOI: 10.1111/j.1600-0854.2010.01124.x

Experimental method

X-RAY DIFFRACTION (2.4 Å)