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TitleStructural and thermodynamic characterization of metal binding in Vps29 from Entamoeba histolytica: implication in retromer function.
Journal, issue, pagesMol. Microbiol., Vol. 106, Page 562-581, Year 2017
Publish dateMar 22, 2017 (structure data deposition date)
AuthorsSrivastava, V.K. / Yadav, R. / Watanabe, N. / Tomar, P. / Mukherjee, M. / Gourinath, S. / Nakada-Tsukui, K. / Nozaki, T. / Datta, S.
External linksMol. Microbiol. / PubMed:28898487
MethodsX-ray diffraction
Resolution1.859 - 2.85 Å
Structure data

PDB-5xce:
Crystal structure of Wild type Vps29 from Entamoeba histolytica
Method: X-RAY DIFFRACTION / Resolution: 1.86 Å

PDB-5xch:
Crystal structure of Wild type Vps29 complexed with Zn+2 from Entamoeba histolytica
Method: X-RAY DIFFRACTION / Resolution: 2.85 Å

PDB-5xcj:
Crystal structure of Vps29 single mutant (D62A) from Entamoeba histolytica
Method: X-RAY DIFFRACTION / Resolution: 1.859 Å

PDB-5xck:
Crystal structure of Vps29 double mutant (D62A/H86A) from Entamoeba histolytica
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-ZN:
Unknown entry

Source
  • entamoeba histolytica (eukaryote)
KeywordsTRANSPORT PROTEIN / Entamoeba histolytica / Vacuolar protein sorting 29 / Metallophosphatase fold / Calcineurin-like phosphoesterase superfamily domain / PROTEIN TRANSPORT

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