1DOS: STRUCTURE OF FRUCTOSE-BISPHOSPHATE ALDOLASE

Citation:
Abstract
The molecular architecture of the Class II E. coli fructose 1,6-bisphosphate aldolase dimer was determined to 1.6 A resolution. The subunit fold corresponds to a singly wound alpha/beta-barrel with an active site located on the beta-barrel carboxyl side of each subunit. In each subunit there are two mutually exclusive zinc metal ion binding sites, 3.2 A apart; the exclusivity is mediated by a conformational transition involving side-chain rotations by chelating histidine residues. A binding site for K+ and NH4+ activators was found near the beta-barrel centre. Although Class I and Class II aldolases catalyse identical reactions, their active sites do not share common amino acid residues, are structurally dissimilar, and from sequence comparisons appear to be evolutionary distinct.
PDB ID: 1DOSDownload
MMDB ID: 6080
PDB Deposition Date: 1996/6/24
Updated in MMDB: 1998/11
Experimental Method:
x-ray diffraction
Resolution: 1.67  Å
Source Organism:
Similar Structures:
Biological Unit for 1DOS: dimeric; determined by author and by software (PISA)
Molecular Components in 1DOS
Label Count Molecule
Proteins (2 molecules)
2
Aldolase Class II(Gene symbol: fbaA)
Molecule annotation
Chemicals (4 molecules)
1
2
2
2
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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