5GN1

Crystal structure of the C-terminal part of Fun30 ATPase domain

Summary for 5GN1

• Entry DOI: 10.2210/pdb5gn1/pdb
• Descriptor: ATP-dependent helicase FUN30 (2 entities in total)
• Functional Keywords: helicase, reca, remodeler, hydrolase
• Biological source: Saccharomyces cerevisiae S288c
• Total number of polymer chains: 4
• Total formula weight: 169627.91

Authors

Jiang, T.,Liu, L. (deposition date: 2016-07-18, release date: 2017-01-11, Last modification date: 2023-11-08)

Primary citation

Liu, L.,Jiang, T.
Crystal structure of the ATPase-C domain of the chromatin remodeller Fun30 from Saccharomyces cerevisiae.
Acta Crystallogr.,Sect.F, 73:9-15, 2017

PubMed Abstract: Fun30 (Function unknown now 30) is a chromatin remodeller belonging to the Snf2 family. It has previously been reported to be a regulator of several cellular activities, including DNA repair, gene silencing and maintenance of chromatin structure. Here, the crystal structure of the Fun30 ATPase-C domain (the C-lobe of the ATPase domain) is reported at 1.95 Å resolution. Although the structure displays overall similarities to those of other Snf2 family members, a new structural module was found to be specific to the Fun30 subfamily. Fun30 ATPase-C was shown be monomeric in solution and showed no detectable affinity for dsDNA.

PubMed: 28045388
DOI: 10.1107/S2053230X16019269

Experimental method

X-RAY DIFFRACTION (1.95 Å)