1ALD: ACTIVITY AND SPECIFICITY OF HUMAN ALDOLASES

Citation:
Abstract
The structure of the type I fructose 1,6-bisphosphate aldolase from human muscle has been extended from 3 A to 2 A resolution. The improvement in the resulting electron density map is such that the 20 or so C-terminal residues, known to be associated with activity and isozyme specificity, have been located. The side-chain of the Schiff's base-forming lysine 229 is located towards the centre of an eight-stranded beta-barrel type structure. The C-terminal "tail" extends from the rim of the beta-barrel towards lysine 229, thus forming part of the active site of the enzyme. This structural arrangement appears to explain the difference in activity and specificity of the three tissue-specific human aldolases and helps with our understanding of the type I aldolase reaction mechanism.
PDB ID: 1ALDDownload
MMDB ID: 55256
PDB Deposition Date: 1991/5/5
Updated in MMDB: 2017/12
Experimental Method:
x-ray diffraction
Resolution: 2  Å
Source Organism:
Similar Structures:
Biological Unit for 1ALD: tetrameric; determined by author and by software (PISA,PQS)
Molecular Components in 1ALD
Label Count Molecule
Proteins (4 molecules)
4
Aldolase a(Gene symbol: ALDOA)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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