×

Network disruptions

We have been experiencing disruptions on our local network which has affected the stability of these web pages. We have been working with IT support team to get this fixed as a matter of urgency and apologise for any inconvenience.

CATH Classification

Domain Context

CATH Clusters

Superfamily P-loop containing nucleotide triphosphate hydrolases
Functional Family

Enzyme Information

3.6.4.12
DNA helicase.
based on mapping to UniProt O51934
ATP + H(2)O = ADP + phosphate.
-!- DNA helicases utilize the energy from ATP hydrolysis to unwind double-stranded DNA. -!- Some of them unwind duplex DNA with a 3' to 5' polarity (1,3,5,8), other show 5' to 3' polarity (10,11,12,13) or unwind DNA in both directions (14,15). -!- Some helicases unwind DNA as well as RNA (4,9). -!- May be identical with EC 3.6.4.13 (RNA helicase).
5.6.2.3
DNA topoisomerase (ATP-hydrolyzing).
based on mapping to UniProt O51934
ATP-dependent breakage, passage and rejoining of double-stranded DNA.
-!- The enzyme can introduce negative superhelical turns into double- stranded circular DNA. -!- One unit has nicking-closing activity, and another catalyzes super- twisting and hydrolysis of ATP (cf. EC 5.6.2.2). -!- Formerly EC 5.99.1.3.

UniProtKB Entries (1)

O51934
RGYR_THEMA
Thermotoga maritima MSB8
Reverse gyrase

PDB Structure

PDB 3P4X
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
The Conformational Flexibility of the Helicase-like Domain from Thermotoga maritima Reverse Gyrase Is Restricted by the Topoisomerase Domain.
Del Toro Duany, Y., Klostermeier, D., Rudolph, M.G.
Biochemistry
CATH-Gene3D is a Global Biodata Core Resource Learn more...