1ojr
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(New page: 200px<br /> <applet load="1ojr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ojr, resolution 1.35Å" /> '''L-RHAMNULOSE-1-PHOS...)
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Revision as of 17:11, 29 October 2007
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L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT E192A)
Overview
The structure of L-rhamnulose-1-phosphate aldolase has been established at, 1.35 A resolution in a crystal form that was obtained by a surface, mutation and has one subunit of the C(4)-symmetric tetramer in the, asymmetric unit. It confirms an earlier 2.7 A resolution structure which, was determined in a complicated crystal form with 20 subunits per, asymmetric unit. The chain fold and the active center are similar to those, of L-fuculose-1-phosphate aldolase and L-ribulose-5-phosphate 4-epimerase., The active center similarity is supported by a structural comparison of, all three enzymes and by the binding mode of the inhibitor, phosphoglycolohydroxamate at the site of the product dihydroxyacetone, phosphate for the two aldolases. The sensitivity of the catalytic rate to, several ... [(full description)]
About this Structure
1OJR is a [Single protein] structure of sequence from [Escherichia coli] with ZN, PO4, 2HA, DIO and GOL as [ligands]. Active as [[1]], with EC number [4.1.2.19]. Full crystallographic information is available from [OCA].
Reference
Structure and catalytic mechanism of L-rhamnulose-1-phosphate aldolase., Kroemer M, Merkel I, Schulz GE, Biochemistry. 2003 Sep 16;42(36):10560-8. PMID:12962479
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