1gt7: Difference between revisions
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L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI
OverviewOverview
The enzyme L-rhamnulose-1-phosphate aldolase catalyzes the reversible, cleavage of L-rhamnulose-1-phosphate to dihydroxyacetone phosphate and, L-lactaldehyde. It is a homotetramer with an M(r) of 30 000 per subunit, and crystallized in space group P3(2)21. The enzyme shows a low sequence, identity of 18% with the structurally known L-fuculose-1-phosphate, aldolase that splits a stereoisomer in a similar reaction. Structure, analysis was initiated with a single heavy-atom derivative measured to 6 A, resolution. The resulting poor electron density, a self-rotation function, and the working hypothesis that both enzymes are C(4) symmetric with, envelopes that resemble one another allowed the location of the 20, protomers of the asymmetric unit. The crystal-packing unit was a, D(4)-symmetric ... [(full description)]
About this StructureAbout this Structure
1GT7 is a [Single protein] structure of sequence from [Escherichia coli] with ZN and PGH as [ligands]. Active as [Rhamnulose-1-phosphate aldolase], with EC number [4.1.2.19]. Structure known Active Site: ZNA. Full crystallographic information is available from [OCA].
ReferenceReference
The structure of L-rhamnulose-1-phosphate aldolase (class II) solved by low-resolution SIR phasing and 20-fold NCS averaging., Kroemer M, Schulz GE, Acta Crystallogr D Biol Crystallogr. 2002 May;58(Pt 5):824-32. Epub 2002, Apr 26. PMID:11976494
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