PDBsum entry 4cdg

Hydrolase

PDB id: 4cdg

Contents

Protein chains

625 a.a.

122 a.a.

Ligands

ADP ×2

Metals

_ZN ×2

PDB id:

4cdg

Name:

Hydrolase

Title:

Crystal structure of the bloom's syndrome helicase blm in complex with nanobody

Structure:

Bloom syndrome protein. Chain: a, b. Fragment: catalytic core, residues 636-1298. Synonym: bloom syndrome helicase, DNA helicase, recq-like type 2, recq2, recq protein-like 3. Engineered: yes. Nanobody. Chain: c, d. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008. Lama glama. Llama. Organism_taxid: 9844. Cell: b-lymphocyte.

Resolution:

2.79Å R-factor: 0.208 R-free: 0.246

Authors:

J.A.Newman,P.Savitsky,C.K.Allerston,A.C.W.Pike,E.Pardon,J.Steyaert, C.H.Arrowsmith,F.Von Delft,C.Bountra,A.Edwards,O.Gileadi

Key ref:

J.A.Newman et al. (2015). Crystal structure of the Bloom's syndrome helicase indicates a role for the HRDC domain in conformational changes. Nucleic Acids Res, 43, 5221-5235. PubMed id: 25901030 DOI: 10.1093/nar/gkv373

Date:

31-Oct-13 Release date: 13-Nov-13

Protein chains

P54132  (BLM_HUMAN) -  RecQ-like DNA helicase BLM from Homo sapiens

Seq: 1417 a.a.

Struc: 625 a.a.

Protein chains

No UniProt id for this chain

Struc: 122 a.a.

Enzyme reactions

• Enzyme class: Chains A, B: E.C.5.6.2.4 - Dna 3'-5' helicase.

DOI no: 10.1093/nar/gkv373

Nucleic Acids Res 43:5221-5235 (2015)

PubMed id: 25901030

Crystal structure of the Bloom's syndrome helicase indicates a role for the HRDC domain in conformational changes.

J.A.Newman, P.Savitsky, C.K.Allerston, A.H.Bizard, Ã.–.Özer, K.Sarlós, Y.Liu, E.Pardon, J.Steyaert, I.D.Hickson, O.Gileadi.

ABSTRACT

Bloom's syndrome helicase (BLM) is a member of the RecQ family of DNA helicases, which play key roles in the maintenance of genome integrity in all organism groups. We describe crystal structures of the BLM helicase domain in complex with DNA and with an antibody fragment, as well as SAXS and domain association studies in solution. We show an unexpected nucleotide-dependent interaction of the core helicase domain with the conserved, poorly characterized HRDC domain. The BLM-DNA complex shows an unusual base-flipping mechanism with unique positioning of the DNA duplex relative to the helicase core domains. Comparison with other crystal structures of RecQ helicases permits the definition of structural transitions underlying ATP-driven helicase action, and the identification of a nucleotide-regulated tunnel that may play a role in interactions with complex DNA substrates.