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

BRENDA support

Literature summary for 2.3.3.16 extracted from

  • Snow, C.; Qi, G.; Hayward, S.
    Essential dynamics sampling study of adenylate kinase: comparison to citrate synthase and implication for the hinge and shear mechanisms of domain motions (2007), Proteins, 67, 325-337.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information mechanism for domain closure. It appears that there is a common barrier between the open- and closed-domain conformations that cannot be overcome in either exploring or targeting simulations. For citrate synthase in the open conformation there are 258 atoms from both domains that are in the domain-contact sets. This increases to only 284 for the closed structure. These atoms come from 61 residues in the open which increases to 66 in the closed. Of these, 57 are common to both open and closed conformations Escherichia coli ?
-
?