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| Novel active site in Escherichia coli fructose 1,6-bisphosphate aldolase |
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| Author(s): Blom NS, Tetreault S, Coulombe R, Sygusch J |
| Source: NATURE STRUCTURAL BIOLOGY Volume: 3 Issue: 10 Pages: 856-862 Published: OCT 1996 |
| Times Cited: 53 References: 51 |
| Abstract: The molecular architecture of the Class II E. coli fructose 1,6-bisphosphate aldolase dimer was determined to 1.6 Angstrom resolution. The subunit fold corresponds to a singly wound alpha/beta-barrel with an active site located on the beta-barret carboxyl side of each subunit. In each subunit there are two mutually exclusive zinc metal ion binding sites, 3.2 Angstrom 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 add residues, are structurally dissimilar, and from sequence comparisons appear to be evolutionary distinct. |
| Document Type: Article |
| Language: English |
Addresses:
1. UNIV MONTREAL, DEPT BIOCHIM, MONTREAL, PQ H3C 3J7 CANADA |
| Publisher: NATURE PUBLISHING CO, 345 PARK AVE SOUTH, NEW YORK, NY 10010-1707 |
| Subject Category: Biochemistry & Molecular Biology; Biophysics; Cell Biology |
| IDS Number: VK993 |
| ISSN: 1072-8368 |
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| | | | | | | | | Record from Web of Science® | | | | | | | | | |