1gjp

From Proteopedia

Revision as of 11:18, 30 October 2007

SCHIFF-BASE COMPLEX OF YEAST 5-AMINOLAEVULINIC ACID DEHYDRATASE WITH 4-OXOSEBACIC ACID

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

1GJP is a [Single protein] structure of sequence from [Saccharomyces cerevisiae] with ZN and 4OX as [ligands]. Active as [Porphobilinogen synthase], with EC number [4.2.1.24]. Structure known Active Site: AC1. 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 Tue Oct 30 13:23:37 2007