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5F0P

Structure of retromer VPS26-VPS35 subunits bound to SNX3 and DMT1(L557M) (SeMet labeled)

Summary for 5F0P
Entry DOI10.2210/pdb5f0p/pdb
Related2FAU 2R17 5F0J 5F0K 5F0L 5F0M
DescriptorVacuolar protein sorting-associated protein 35, Vacuolar protein sorting-associated protein 26A, Sorting nexin-3, ... (9 entities in total)
Functional Keywordsprotein transport, retromer, sorting nexin
Biological sourceHomo sapiens (Human)
More
Cellular locationCytoplasm: Q96QK1 O75436
Early endosome : O60493
Isoform 2: Cell membrane ; Multi- pass membrane protein . Endosome membrane ; Multi-pass membrane protein : P49281
Total number of polymer chains4
Total formula weight114930.16
Authors
Lucas, M.,Gershlick, D.,Vidaurrazaga, A.,Rojas, A.L.,Bonifacino, J.S.,Hierro, A. (deposition date: 2015-11-27, release date: 2016-12-07, Last modification date: 2024-10-23)
Primary citationLucas, M.,Gershlick, D.C.,Vidaurrazaga, A.,Rojas, A.L.,Bonifacino, J.S.,Hierro, A.
Structural Mechanism for Cargo Recognition by the Retromer Complex.
Cell, 167:1623-1635.e14, 2016
Cited by
PubMed Abstract: Retromer is a multi-protein complex that recycles transmembrane cargo from endosomes to the trans-Golgi network and the plasma membrane. Defects in retromer impair various cellular processes and underlie some forms of Alzheimer's disease and Parkinson's disease. Although retromer was discovered over 15 years ago, the mechanisms for cargo recognition and recruitment to endosomes have remained elusive. Here, we present an X-ray crystallographic analysis of a four-component complex comprising the VPS26 and VPS35 subunits of retromer, the sorting nexin SNX3, and a recycling signal from the divalent cation transporter DMT1-II. This analysis identifies a binding site for canonical recycling signals at the interface between VPS26 and SNX3. In addition, the structure highlights a network of cooperative interactions among the VPS subunits, SNX3, and cargo that couple signal-recognition to membrane recruitment.
PubMed: 27889239
DOI: 10.1016/j.cell.2016.10.056
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.78 Å)
Structure validation

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数据于2024-11-06公开中

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