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4BX8

Human Vps33A

Summary for 4BX8
Entry DOI10.2210/pdb4bx8/pdb
Related4BX9
DescriptorVACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 33A, CHLORIDE ION (3 entities in total)
Functional Keywordsprotein transport, hops, membrane trafficking, sec1/munc18 proteins, tethering
Biological sourceHOMO SAPIENS (HUMAN)
Total number of polymer chains2
Total formula weight138503.61
Authors
Graham, S.C.,Wartosch, L.,Gray, S.R.,Scourfield, E.J.,Deane, J.E.,Luzio, J.P.,Owen, D.J. (deposition date: 2013-07-09, release date: 2013-07-24, Last modification date: 2024-05-08)
Primary citationGraham, S.C.,Wartosch, L.,Gray, S.R.,Scourfield, E.J.,Deane, J.E.,Luzio, J.P.,Owen, D.J.
Structural Basis of Vps33A Recruitment to the Human Hops Complex by Vps16.
Proc.Natl.Acad.Sci.USA, 110:13345-, 2013
Cited by
PubMed Abstract: The multisubunit homotypic fusion and vacuole protein sorting (HOPS) membrane-tethering complex is required for late endosome-lysosome and autophagosome-lysosome fusion in mammals. We have determined the crystal structure of the human HOPS subunit Vps33A, confirming its identity as a Sec1/Munc18 family member. We show that HOPS subunit Vps16 recruits Vps33A to the human HOPS complex and that residues 642-736 are necessary and sufficient for this interaction, and we present the crystal structure of Vps33A in complex with Vps16(642-736). Mutations at the binding interface disrupt the Vps33A-Vps16 interaction both in vitro and in cells, preventing recruitment of Vps33A to the HOPS complex. The Vps33A-Vps16 complex provides a structural framework for studying the association between Sec1/Munc18 proteins and tethering complexes.
PubMed: 23901104
DOI: 10.1073/PNAS.1307074110
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

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