2ald: Difference between revisions

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 flexible C-terminal region. This is also the region where the, native and complex structures exhibit differences. The conformational, changes between native and complex structure are not large, but the, observed complex does not involve the full formation of the Schiff's base, intermediate, and suggests a preliminary hydrogen-bonded Michaelis complex, before the formation of the covalent complex.

2ALD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Fructose-bisphosphate_aldolase Fructose-bisphosphate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.13 4.1.2.13] Structure known Active Site: SBL. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2ALD OCA].  

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