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1ald
From Proteopedia
| 1ald, resolution 2.00Å () | |||||||||
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| Activity: | Fructose-bisphosphate aldolase, with EC number 4.1.2.13 | ||||||||
| Domains: | FBP_aldolase_I_a | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
ACTIVITY AND SPECIFICITY OF HUMAN ALDOLASES
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.
Activity and specificity of human aldolases., Gamblin SJ, Davies GJ, Grimes JM, Jackson RM, Littlechild JA, Watson HC, J Mol Biol. 1991 Jun 20;219(4):573-6. PMID:2056525
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1ALD is a 1 chain structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Gamblin SJ, Davies GJ, Grimes JM, Jackson RM, Littlechild JA, Watson HC. Activity and specificity of human aldolases. J Mol Biol. 1991 Jun 20;219(4):573-6. PMID:2056525
Page seeded by OCA on Tue Feb 17 04:40:12 2009
