PDBsum entry 2chv

DNA binding protein

PDB id: 2chv

Contents

Protein chains

(+ 0 more) 314 a.a. *

* Residue conservation analysis

PDB id:

2chv

Name:

DNA binding protein

Title:

Replication factor c adpnp complex

Structure:

Replication factor c small subunit. Chain: a, b, c, d, e, f. Synonym: replication factor c, rfc small subunit, clamp loader small subunit, afrfc small subunit, afrfcsm. Engineered: yes

Source:

Archaeoglobus fulgidus. Organism_taxid: 2234. Expressed in: escherichia coli. Expression_system_taxid: 562

Biol. unit:

Hexamer (from PDB file)

Resolution:

4.00Å R-factor: 0.492 R-free: 0.498

Authors:

A.Seybert,M.R.Singleton,N.Cook,D.R.Hall,D.B.Wigley

Key ref:

A.Seybert et al. (2006). Communication between subunits within an archaeal clamp-loader complex. EMBO J, 25, 2209-2218. PubMed id: 16628222 DOI: 10.1038/sj.emboj.7601093

Date:

16-Mar-06 Release date: 06-Jun-06

Protein chains

O28219  (RFCS_ARCFU) -  Replication factor C small subunit from Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)

Seq: 319 a.a.

Struc: 314 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1038/sj.emboj.7601093

EMBO J 25:2209-2218 (2006)

PubMed id: 16628222

Communication between subunits within an archaeal clamp-loader complex.

A.Seybert, M.R.Singleton, N.Cook, D.R.Hall, D.B.Wigley.

ABSTRACT

We have investigated the communication between subunits in replication factor C (RFC) from Archaeoglobus fulgidus. Mutation of the proposed arginine finger in the small subunits results in a complex that can still bind ATP but has impaired clamp-loading activity, a process that normally only requires binding of nucleotide. The small subunit alone forms a hexameric ring that is six-fold symmetric in the absence of ATP. However, this symmetry is broken when the nucleotide is bound to the complex. A conformational change associated with nucleotide binding may relate to the opening of PCNA rings by RFC during the loading reaction. The structures also reveal the importance of the N-terminal helix of each subunit at the ATP-binding site. Analysis of mutant protein complexes containing subunits lacking this N-terminal helix reveals key distinct regulatory roles during clamp loading that are different for the large and small subunits in the RFC complex.

Selected figure(s)

Figure 2.
Figure 2 Overall fold of a monomer of the A. fulgidus RFC small subunit. The N-terminal domain 1 is coloured in red, domain 2 is blue and domain 3 is green. The inset shows a zoom in the ATP-binding site, with difference (F[o]-F[c]) electron density for one of the ADPNP molecules bound to the complex.

Figure 5.
Figure 5 (A) The location of the N-terminal helix (RFC box II) within the ATP-binding site. (B) Diagram showing how the N-terminal helix blocks access of the arginine finger (Arg152) to the ATP-binding site.

The above figures are reprinted from an Open Access publication published by Macmillan Publishers Ltd: EMBO J (2006, 25, 2209-2218) copyright 2006.

Figures were selected by an automated process.