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2CAZ

ESCRT-I core

Summary for 2CAZ
Entry DOI10.2210/pdb2caz/pdb
Related1UZX
DescriptorSUPPRESSOR PROTEIN STP22 OF TEMPERATURE-SENSITIVE ALPHA-FACTOR RECEPTOR AND ARGININE PERMEASE, VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN VPS28, PROTEIN SRN2 (3 entities in total)
Functional Keywordsprotein transport, escrt, mvb, multivesicular bodies, endosome, lysosome, ph domain, protein sorting, vesicle trafficking, ubiquitin, phosphoinositide, ptdins3p, vps23, vps28, vps37, vps36, coiled coil, ubl conjugation pathway
Biological sourceSACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
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Total number of polymer chains6
Total formula weight74661.12
Authors
Gill, D.J.,Teo, H.,Sun, J.,Perisic, O.,Veprintsev, D.B.,Vallis, Y.,Emr, S.D.,Williams, R.L. (deposition date: 2005-12-23, release date: 2006-04-07, Last modification date: 2024-05-08)
Primary citationTeo, H.,Gill, D.J.,Sun, J.,Perisic, O.,Veprintsev, D.B.,Wallis, Y.,Emr, S.D.,Williams, R.L.
Escrt-I Core and Escrt-II Glue Domain Structures Reveal Role for Glue in Linking to Escrt-I and Membranes.
Cell(Cambridge,Mass.), 125:99-, 2006
Cited by
PubMed Abstract: ESCRT complexes form the main machinery driving protein sorting from endosomes to lysosomes. Currently, the picture regarding assembly of ESCRTs on endosomes is incomplete. The structure of the conserved heterotrimeric ESCRT-I core presented here shows a fan-like arrangement of three helical hairpins, each corresponding to a different subunit. Vps23/Tsg101 is the central hairpin sandwiched between the other subunits, explaining the critical role of its "steadiness box" in the stability of ESCRT-I. We show that yeast ESCRT-I links directly to ESCRT-II, through a tight interaction of Vps28 (ESCRT-I) with the yeast-specific zinc-finger insertion within the GLUE domain of Vps36 (ESCRT-II). The crystal structure of the GLUE domain missing this insertion reveals it is a split PH domain, with a noncanonical lipid binding pocket that binds PtdIns3P. The simultaneous and reinforcing interactions of ESCRT-II GLUE domain with membranes, ESCRT-I, and ubiquitin are critical for ubiquitinated cargo progression from early to late endosomes.
PubMed: 16615893
DOI: 10.1016/J.CELL.2006.01.047
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.6 Å)
Structure validation

226707

数据于2024-10-30公开中

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