1e5m

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1e5m, resolution 1.54Å

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BETA KETOACYL ACYL CARRIER PROTEIN SYNTHASE II (KASII) FROM SYNECHOCYSTIS SP.

Overview

Condensing enzymes, catalyzing the formation of carbon-carbon bonds in, several biosynthetic pathways, have lately been recognized as potential, drug targets against cancer and tuberculosis, as crucial for combinatorial, biosynthesis of antibiotics and related compounds, and as determinants of, plant oil composition. beta-Ketoacyl-ACP synthases (KAS) are the, condensing enzymes present in the fatty acid biosynthesis pathway and are, able to elongate an acyl chain bound to either co-enzyme A (CoA) or acyl, carrier protein (ACP) with a two-carbon unit derived from malonyl-ACP., Several isoforms of KAS with different substrate specificity are present, in most species. We have determined the crystal structure of KAS II from, Synechocystis sp. PCC 6803 to 1.54 A resolution giving a detailed, ... [(full description)]

About this Structure

1E5M is a [Single protein] structure of sequence from [Synechocystis sp.]. Active as [Beta-ketoacyl-acyl-carrier-protein synthase I], with EC number [2.3.1.41]. Structure known Active Site: CYS. Full crystallographic information is available from [OCA].

Reference

The crystal structure of beta-ketoacyl-acyl carrier protein synthase II from Synechocystis sp. at 1.54 A resolution and its relationship to other condensing enzymes., Moche M, Dehesh K, Edwards P, Lindqvist Y, J Mol Biol. 2001 Jan 19;305(3):491-503. PMID:11152607

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