PDBsum entry 3aaf

DNA binding protein/DNA

PDB id: 3aaf

Contents

Protein chain

109 a.a. *

DNA/RNA

Ligands

ACT ×2

Waters ×338

* Residue conservation analysis

PDB id:

3aaf

Name:

DNA binding protein/DNA

Title:

Structure of wrn rqc domain bound to double-stranded DNA

Structure:

Werner syndrome atp-dependent helicase. Chain: a, b. Fragment: recq c-terminal (rqc) domain. Synonym: werner syndrome protein, wrn. Engineered: yes. DNA (5'-d( Ap Cp Cp Cp Tp Ap Ap Tp Tp Ap Gp Gp Gp T)-3'). Chain: c, d. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes

Resolution:

1.90Å R-factor: 0.213 R-free: 0.244

Authors:

K.Kitano,T.Hakoshima

Key ref:

K.Kitano et al. (2010). Structural basis for DNA strand separation by the unconventional winged-helix domain of RecQ helicase WRN. Structure, 18, 177-187. PubMed id: 20159463

Date:

16-Nov-09 Release date: 16-Feb-10

Protein chains

Q14191  (WRN_HUMAN) -  Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN from Homo sapiens

Seq: 1432 a.a.

Struc: 109 a.a.

DNA/RNA chains

A-C-C-C-T-A-A-T-T-A-G-G-G-T 14 bases

A-C-C-C-T-A-A-T-T-A-G-G-G-T 14 bases

Enzyme reactions

• Enzyme class 1: E.C.3.1.-.-
• Enzyme class 2: E.C.3.6.4.12 - Dna helicase.
• Reaction: ATP + H2O = ADP + phosphate + H⁺

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

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

reference

Structure 18:177-187 (2010)

PubMed id: 20159463

Structural basis for DNA strand separation by the unconventional winged-helix domain of RecQ helicase WRN.

K.Kitano, S.Y.Kim, T.Hakoshima.

ABSTRACT

The RecQ family of DNA helicases including WRN (Werner syndrome protein) and BLM (Bloom syndrome protein) protects the genome against deleterious changes. Here we report the cocrystal structure of the RecQ C-terminal (RQC) domain of human WRN bound to a DNA duplex. In the complex, the RQC domain specifically interacted with a blunt end of the duplex and, surprisingly, unpaired a Watson-Crick base pair in the absence of an ATPase domain. The beta wing, an extended hairpin motif that is characteristic of winged-helix motifs, was used as a "separating knife" to wedge between the first and second base pairs, whereas the recognition helix, a principal component of helix-turn-helix motifs that are usually embedded within DNA grooves, was unprecedentedly excluded from the interaction. Our results demonstrate a function of the winged-helix motif central to the helicase reaction, establishing the first structural paradigm concerning the DNA structure-specific activities of the RecQ helicases.