3ULB

Crystal structure of the pleckstrin homology domain of Saccharomyces cerevisiae Avo1, a TORC2 subunit, in the P212121 crystal form

Summary for 3ULB

• Entry DOI: 10.2210/pdb3ulb/pdb
• Related: 3ULC
• Descriptor: Target of rapamycin complex 2 subunit AVO1 (2 entities in total)
• Functional Keywords: ph domain, membrane localization, membrane protein
• Biological source: Saccharomyces cerevisiae (yeast)
• Cellular location: Cell membrane ; Peripheral membrane protein ; Cytoplasmic side : Q08236
• Total number of polymer chains: 2
• Total formula weight: 29217.47

Authors

Pan, D.,Matsuura, Y. (deposition date: 2011-11-10, release date: 2012-04-11, Last modification date: 2023-11-01)

Primary citation

Pan, D.,Matsuura, Y.
Structures of the pleckstrin homology domain of Saccharomyces cerevisiae Avo1 and its human orthologue Sin1, an essential subunit of TOR complex 2
Acta Crystallogr.,Sect.F, 68:386-392, 2012

PubMed Abstract: In eukaryotes, multiprotein complexes termed TOR complex 1 (TORC1) and TOR complex 2 (TORC2) function as major regulators of cell growth, metabolism and ageing. The C-terminal domain of the Saccharomyces cerevisiae TORC2 component Avo1 is required for plasma-membrane localization of TORC2 and is essential for yeast viability. X-ray crystal structures of the C-terminal domain of Avo1 and of its human orthologue Sin1 have been determined. The structures show that the C-termini of Avo1 and Sin1 both have the pleckstrin homology (PH) domain fold. Comparison with known PH-domain structures suggests a putative binding site for phosphoinositides.

PubMed: 22505404
DOI: 10.1107/S1744309112007178

Experimental method

X-RAY DIFFRACTION (1.9 Å)