1ald

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spinqualitylabelsall models 1ald, resolution 2.0Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

ACTIVITY AND SPECIFICITY OF HUMAN ALDOLASES

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

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.

Disease

Known disease associated with this structure: Aldolase A deficiency OMIM:[103850]

About this Structure

1ALD is a Single protein structure of sequence from Homo sapiens. Active as Fructose-bisphosphate aldolase, with EC number 4.1.2.13 Full crystallographic information is available from OCA.

Reference

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

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