Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 5.6.2.3 extracted from

  • Bhattacharyya, B.; Keck, J.L.
    Grip it and rip it: structural mechanisms of DNA helicase substrate binding and unwinding (2014), Protein Sci., 23, 1498-1507.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.6.2.3

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure analysis, PDB ID 4C30 Deinococcus radiodurans

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Deinococcus radiodurans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O Deinococcus radiodurans
-
 ADP + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Deinococcus radiodurans Q9RT63
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O
-
 Deinococcus radiodurans ADP + phosphate
-
 ?
ATP + H2O the SF1A helicase shows direct DNA binding by conserved aromatic (Trp or Phe) and electropositive (Arg) residues within the ARLs via stacking with ssDNA bases and gripping the phosphodiester backbone, respectively Deinococcus radiodurans ADP + phosphate
-
 ?

Subunits

Subunits Comment Organism
More structure-function relationship Deinococcus radiodurans

Synonyms

Synonyms Comment Organism
ATP-dependent RecD-like DNA helicase
-
 Deinococcus radiodurans
SF1 helicase
-
 Deinococcus radiodurans
UvrD
-
 Deinococcus radiodurans

General Information

General Information Comment Organism
evolution superfamilies 1 and 2 (SF1 and SF2) comprise the largest number of helicase families and members are involved in a wide array of cellular functions that require manipulation of DNA or RNA structures, the helicases belong to the AAA+ ATPases. Helicase superfamilies can also be subdivided into those that translocate along DNA and unwind in a 3'-5' direction, e.g., SF1A, or a 5'-3 direction, e.g., SF1B. SF1 and SF2 helicases can be identified based on evolutionary conservation of seven sequence motifs (I, Ia, II-VI) that are required for ATP binding/hydrolysis, nucleic acid binding, and/or translocation. SF1 and SF2 helicases include a conserved core helicase domain that is comprised of two subdomains that share similarity with RecA ATPase/recombinase enzyme family Deinococcus radiodurans
additional information structure comparisons of SF1 and SF2 helicases, SF1 and SF2 helicase domains structures and substrate-bound SF1 and SF2 helicase structures, structure-function relationship, overview Deinococcus radiodurans
physiological function aromatic-rich loops as coupling motifs that link DNA binding and ATP hydrolysis, the conserved SF1 and SF2 helicase motifs mediate ATP binding and hydrolysis and convert the released chemical energy into the mechanical energy required for translocation and DNA unwinding Deinococcus radiodurans