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2ald
From Proteopedia
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(New page: 200px<br /> <applet load="2ald" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ald, resolution 2.1Å" /> '''HUMAN MUSCLE ALDOLAS...)
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Revision as of 14:21, 29 October 2007
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HUMAN MUSCLE ALDOLASE
Overview
Fructose 1,6-bisphosphate aldolase catalyzes the reversible cleavage of, fructose 1,6-bisphosphate and fructose 1-phosphate to dihydroxyacetone, phosphate and either glyceraldehyde 3-phosphate or glyceraldehyde, respectively. Catalysis involves the formation of a Schiff's base, intermediate formed at the epsilon-amino group of Lys229. The existing, apo-enzyme structure was refined using the crystallographic free-R-factor, and maximum likelihood methods that have been shown to give improved, structural results that are less subject to model bias. Crystals were also, soaked with the natural substrate (fructose 1,6-bisphosphate), and the, crystal structure of this complex has been determined to 2.8 A. The apo, structure differs from the previous Brookhaven-deposited structure (1ald), in the ... [(full description)]
About this Structure
2ALD is a [Single protein] structure of sequence from [Homo sapiens]. Active as [[1]], with EC number [4.1.2.13]. Full crystallographic information is available from [OCA].
Reference
Crystal structure of human muscle aldolase complexed with fructose 1,6-bisphosphate: mechanistic implications., Dalby A, Dauter Z, Littlechild JA, Protein Sci. 1999 Feb;8(2):291-7. PMID:10048322
Page seeded by OCA on Mon Oct 29 16:26:33 2007
