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1eb3
From Proteopedia
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(New page: 200px<br /> <applet load="1eb3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eb3, resolution 1.75Å" /> '''YEAST 5-AMINOLAEVUL...)
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Revision as of 15:36, 29 October 2007
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YEAST 5-AMINOLAEVULINIC ACID DEHYDRATASE 4,7-DIOXOSEBACIC ACID COMPLEX
Overview
The structures of 5-aminolaevulinic acid dehydratase complexed with two, irreversible inhibitors (4-oxosebacic acid and 4,7-dioxosebacic acid) have, been solved at high resolution. Both inhibitors bind by forming a Schiff, base link with Lys 263 at the active site. Previous inhibitor binding, studies have defined the interactions made by only one of the two, substrate moieties (P-side substrate) which bind to the enzyme during, catalysis. The structures reported here provide an improved definition of, the interactions made by both of the substrate molecules (A- and P-side, substrates). The most intriguing result is the novel finding that, 4,7-dioxosebacic acid forms a second Schiff base with the enzyme involving, Lys 210. It has been known for many years that P-side substrate forms a, ... [(full description)]
About this Structure
1EB3 is a [Single protein] structure of sequence from [Saccharomyces cerevisiae] with ZN and DSB as [ligands]. Active as [[1]], with EC number [4.2.1.24]. Full crystallographic information is available from [OCA].
Reference
The X-ray structure of yeast 5-aminolaevulinic acid dehydratase complexed with two diacid inhibitors., Erskine PT, Coates L, Newbold R, Brindley AA, Stauffer F, Wood SP, Warren MJ, Cooper JB, Shoolingin-Jordan PM, Neier R, FEBS Lett. 2001 Aug 17;503(2-3):196-200. PMID:11513881
Page seeded by OCA on Mon Oct 29 17:40:55 2007
