Structural complexity of the co-chaperone SGTA: a conserved C-terminal region is implicated in dimerization and substrate quality control.

Martínez-Lumbreras S, Krysztofinska EM, Thapaliya A, Spilotros A, Matak-Vinkovic D, Salvadori E, Roboti P, Nyathi Y, Muench JH, Roessler MM, Svergun DI, High S, Isaacson RL
BMC Biol 16(1):76 (2018 Jul 11)

PMID: 29996828 doi: 10.1186/s12915-018-0542-3

Submitted to SASBDB: 2018 May 2 Published in SASBDB: 2018 Jun 11

SASDDB6 – Small glutamine-rich tetratricopeptide repeat-containing protein alpha (full length; SGTA_FL) Sample: Small glutamine-rich tetratricopeptide repeat-containing protein alpha full length dimer, 68 kDa Homo sapiens protein Buffer: 10 mM potassium phosphate, 100 mM NaCl, pH: 6 Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jun 5 RgGuinier 4.2 nm

SASDDC6 – Small glutamine-rich tetratricopeptide repeat-containing protein alpha (N-terminal-TPR domains; SGTA_NT) Sample: Small glutamine-rich tetratricopeptide repeat-containing protein alpha Nterminal-TPR domains dimer, 47 kDa Homo sapiens protein Buffer: 10 mM potassium phosphate, 100 mM NaCl, pH: 6 Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jun 5 RgGuinier 3.6 nm