1dos
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(New page: 200px<br /><applet load="1dos" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dos, resolution 1.67Å" /> '''STRUCTURE OF FRUCTOS...)
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Revision as of 11:19, 20 November 2007
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STRUCTURE OF FRUCTOSE-BISPHOSPHATE ALDOLASE
Overview
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.
About this Structure
1DOS is a Single protein structure of sequence from Escherichia coli with ZN and NH4 as ligands. Active as Fructose-bisphosphate aldolase, with EC number 4.1.2.13 Full crystallographic information is available from OCA.
Reference
Novel active site in Escherichia coli fructose 1,6-bisphosphate aldolase., Blom NS, Tetreault S, Coulombe R, Sygusch J, Nat Struct Biol. 1996 Oct;3(10):856-62. PMID:8836102
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