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

BRENDA support

Literature summary for 4.1.2.13 extracted from

  • Izard, T.; Sygusch, J.
    Induced fit movements and metal cofactor selectivity of class II aldolases: structure of Thermus aquaticus fructose-1,6-bisphosphate aldolase (2004), J. Biol. Chem., 279, 11825-11833.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Thermus aquaticus

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ the quaternary structure reveals a tetramer composed of two dimers related by a 2-fold axis. Taq FBP aldolase subunits exhibit two distinct conformational states corresponding to loop regions that are in either open or closed position with respect to the active site. Loop closure remodels the disposition of chelating active site histidine residues. In subunits corresponding to the open conformation, the metal cofactor, Co2+, is sequestered in the active site, whereas for subunits in the closed conformation, the metal cation exchanges between two mutually exclusive binding loci, corresponding to a site at the active site surface and an interior site vicinal to the metal-binding site in the open conformation Thermus aquaticus

Organism

Organism UniProt Comment Textmining
Thermus aquaticus
-
-
-