5GN1

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

PDB DOI: https://doi.org/10.2210/pdb5GN1/pdb

Classification: HYDROLASE
Organism(s): Saccharomyces cerevisiae S288C
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2016-07-18 Released: 2017-01-11
Deposition Author(s): Jiang, T., Liu, L.
Funding Organization(s): Chinese Academy of Science

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.95 Å
R-Value Free: 0.216
R-Value Work: 0.187
R-Value Observed: 0.188

wwPDB Validation 3D Report Full Report

This is version 1.3 of the entry. See complete history.

Literature

Crystal structure of the ATPase-C domain of the chromatin remodeller Fun30 from Saccharomyces cerevisiae.

Liu, L., Jiang, T.

(2017) Acta Crystallogr F Struct Biol Commun 73: 9-15

PubMed: 28045388 Search on PubMedSearch on PubMed Central
DOI: https://doi.org/10.1107/S2053230X16019269
Primary Citation of Related Structures:
5GN1

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.

Organizational Affiliation

National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Datun Road, Chaoyang District, Beijing 100101, People's Republic of China.

Macromolecule Content

Total Structure Weight: 169.63 kDa
Atom Count: 11,466
Modelled Residue Count: 1,240
Deposited Residue Count: 1,464
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
ATP-dependent helicase FUN30	A, B, C, D	366	Saccharomyces cerevisiae S288C	Mutation(s): 0 Gene Names: FUN30 EC: 3.6.4.12
UniProt
Find proteins for P31380 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c)) Explore P31380 Go to UniProtKB: P31380
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P31380
Sequence Annotations Expand
Reference Sequence

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.95 Å
R-Value Free: 0.216
R-Value Work: 0.187
R-Value Observed: 0.188
Space Group: C 1 2 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 114.431	α = 90
b = 118.394	β = 107.28
c = 111.578	γ = 90

Software Package:

Software Name	Purpose
PHENIX	refinement
HKL-2000	data reduction
HKL-2000	data scaling
PHENIX	model building
PHASER	phasing

Structure Validation

View Full Validation Report

Entry History & Funding Information

Deposition Data

Released Date: 2017-01-11

Deposition Author(s):

Jiang, T.

Liu, L.

Funding Organization	Location	Grant Number
Chinese Academy of Science	China	XDB08010301

Revision History (Full details and data files)

Version 1.0: 2017-01-11
Type: Initial release
Version 1.1: 2017-09-27
Changes: Data collection
Version 1.2: 2020-01-01
Changes: Database references
Version 1.3: 2023-11-08
Changes: Data collection, Database references, Refinement description