5AMS

Crystal structure of Sqt1

Summary for 5AMS

• Entry DOI: 10.2210/pdb5ams/pdb
• Descriptor: RIBOSOME ASSEMBLY PROTEIN SQT1 (2 entities in total)
• Functional Keywords: chaperone, sqt1, ribosome, ul16
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• Total number of polymer chains: 2
• Total formula weight: 94403.21

Authors

Frenois, F.,Legrand, P.,Fribourg, S. (deposition date: 2015-08-31, release date: 2016-01-13, Last modification date: 2024-05-08)

Primary citation

Frenois, F.,Legrand, P.,Fribourg, S.
Sqt1P is an Eight-Bladed Wd40 Protein
Acta Crystallogr.,Sect.F, 72:59-, 2016

PubMed Abstract: Ribosome biogenesis in eukaryotes is a complex and highly orchestrated process involving more than 200 accessory factors in addition to ribosomal RNAs and ribosomal proteins. Among the many factors involved, Sqt1p has been reported to specifically bind to uL16 and to act as a chaperone. The crystal structure of full-length Sqt1p from the yeast Saccharomyces cerevisiae has been solved at 3.35 Å resolution. A SAD experiment at the Se K edge and an S-SAD experiment on the same selenomethionine-substituted protein crystal allowed unambiguous positioning of the selenomethionine and Cys residues. On the basis of the atomic structure of Sqt1p, the potential residues involved in uL16 interaction were identified and tested.

PubMed: 26750486
DOI: 10.1107/S2053230X15024097

Experimental method

X-RAY DIFFRACTION (3.35 Å)