PDBsum entry 5iy0

Replication DNA binding protein

PDB id

5iy0

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Contents

			Protein chains

					(+ 0 more) 253 a.a.

			Metals

					_ZN ×6

PDB id:

5iy0

Links

Name:

Replication DNA binding protein

Title:

Pfmcm n-terminal domain double hexamer

Structure:

Cell division control protein 21. Chain: a, b, c, d, e, f. Fragment: n-terminal domain (unp residues 2-256). Engineered: yes

Source:

Pyrococcus furiosus. Organism_taxid: 186497. Strain: atcc 43587 / dsm 3638 / jcm 8422 / vc1. Gene: pf0482. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

3.00Å

R-factor:

0.205

R-free:

0.223

Authors:

M.Meagher,E.J.Enemark

Key ref:

M.Meagher and E.J.Enemark (2016). Structure of a double hexamer of the Pyrococcus furiosus minichromosome maintenance protein N-terminal domain. Acta Crystallogr F Struct Biol Commun, 72, 545-551. PubMed id: 27380371 DOI: 10.1107/S2053230X1600858X

Date:

23-Mar-16

Release date:

13-Jul-16

PROCHECK

	Headers

	References

Protein chains

Q8U3I4 (Q8U3I4_PYRFU) - DNA helicase from Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)

Seq: Struc:

Seq: Struc:

Seq: Struc:					1049 a.a. 253 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 1 residue position (black cross)



		Enzyme reactions

Enzyme class:

E.C.3.6.4.12 - Dna helicase.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

Reaction:

ATP + H2O = ADP + phosphate + H⁺

ATP	+	H2O	=	ADP	+	phosphate	+	H(+)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1107/S2053230X1600858X	Acta Crystallogr F Struct Biol Commun 72:545-551 (2016)
PubMed id: 27380371

Structure of a double hexamer of the Pyrococcus furiosus minichromosome maintenance protein N-terminal domain.
M.Meagher, E.J.Enemark.

ABSTRACT

The crystal structure of the N-terminal domain of the Pyrococcus furiosus minichromosome maintenance (MCM) protein as a double hexamer is described. The MCM complex is a ring-shaped helicase that unwinds DNA at the replication fork of eukaryotes and archaea. Prior to replication initiation, the MCM complex assembles as an inactive double hexamer at specific sites of DNA. The presented structure is highly consistent with previous MCM double-hexamer structures and shows two MCM hexamers with a head-to-head interaction mediated by the N-terminal domain. Minor differences include a diminished head-to-head interaction and a slightly reduced inter-hexamer rotation.