5f0p

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

Structural highlights

5f0p is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.78Å
Ligands:EDO, GOL, MSE, SO4, ZN
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

NRAM2_HUMAN Microcytic anemia with liver iron overload. The disease is caused by mutations affecting the gene represented in this entry.

Function

NRAM2_HUMAN Important in metal transport, in particular iron. Can also transport manganese, cobalt, cadmium, nickel, vanadium and lead. Involved in apical iron uptake into duodenal enterocytes. Involved in iron transport from acidified endosomes into the cytoplasm of erythroid precursor cells. May play an important role in hepatic iron accumulation and tissue iron distribution. May serve to import iron into the mitochondria.[1] [2] [3] [4]

Publication Abstract from PubMed

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.

Structural Mechanism for Cargo Recognition by the Retromer Complex.,Lucas M, Gershlick DC, Vidaurrazaga A, Rojas AL, Bonifacino JS, Hierro A Cell. 2016 Dec 1;167(6):1623-1635.e14. doi: 10.1016/j.cell.2016.10.056. Epub 2016, Nov 23. PMID:27889239[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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See Also

References

  1. ↑ Mackenzie B, Takanaga H, Hubert N, Rolfs A, Hediger MA. Functional properties of multiple isoforms of human divalent metal-ion transporter 1 (DMT1). Biochem J. 2007 Apr 1;403(1):59-69. PMID:17109629 doi:http://dx.doi.org/10.1042/BJ20061290
  2. ↑ Wolff NA, Ghio AJ, Garrick LM, Garrick MD, Zhao L, Fenton RA, Thevenod F. Evidence for mitochondrial localization of divalent metal transporter 1 (DMT1). FASEB J. 2014 May;28(5):2134-45. doi: 10.1096/fj.13-240564. Epub 2014 Jan 21. PMID:24448823 doi:http://dx.doi.org/10.1096/fj.13-240564
  3. ↑ Ehrnstorfer IA, Geertsma ER, Pardon E, Steyaert J, Dutzler R. Crystal structure of a SLC11 (NRAMP) transporter reveals the basis for transition-metal ion transport. Nat Struct Mol Biol. 2014 Oct 19. doi: 10.1038/nsmb.2904. PMID:25326704 doi:http://dx.doi.org/10.1038/nsmb.2904
  4. ↑ Yanatori I, Yasui Y, Noguchi Y, Kishi F. Inhibition of iron uptake by ferristatin II is exerted through internalization of DMT1 at the plasma membrane. Cell Biol Int. 2015 Apr;39(4):427-34. doi: 10.1002/cbin.10403. Epub 2015 Jan 5. PMID:25491917 doi:http://dx.doi.org/10.1002/cbin.10403
  5. ↑ Lucas M, Gershlick DC, Vidaurrazaga A, Rojas AL, Bonifacino JS, Hierro A. Structural Mechanism for Cargo Recognition by the Retromer Complex. Cell. 2016 Dec 1;167(6):1623-1635.e14. doi: 10.1016/j.cell.2016.10.056. Epub 2016, Nov 23. PMID:27889239 doi:http://dx.doi.org/10.1016/j.cell.2016.10.056

Contents


PDB ID 5f0p

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OCA

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