2cfb

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2cfb, resolution 2.85Å

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GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE FROM THERMOSYNECHOCOCCUS ELONGATUS

Overview

Glutamate-1-semialdehyde 2,1-aminomutase (GSAM) is the second enzyme in, the C(5) pathway of tetrapyrrole biosynthesis found in most bacteria, in, archaea and in plants. It catalyzes the transamination of, glutamate-1-semialdehyde to 5-aminolevulinic acid (ALA) in a pyridoxal, 5'-phosphate (PLP)-dependent manner. We present the crystal structure of, GSAM from the thermophilic cyanobacterium Thermosynechococcus elongatus, (GSAM(Tel)) in its PLP-bound form at 2.85A resolution. GSAM(Tel) is a, symmetric homodimer, whereas GSAM from Synechococcus (GSAM(Syn)) has been, described as asymmetric. The symmetry of GSAM(Tel) thus challenges the, previously proposed negative cooperativity between monomers of this, enzyme. Furthermore, GSAM(Tel) reveals an extensive flexible region at the, interface ... [(full description)]

About this Structure

2CFB is a [Single protein] structure of sequence from [Synechococcus elongatus] with PLR as [ligand]. Active as [Glutamate-1-semialdehyde 2,1-aminomutase], with EC number [5.4.3.8]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Evolutionary relationship between initial enzymes of tetrapyrrole biosynthesis., Schulze JO, Schubert WD, Moser J, Jahn D, Heinz DW, J Mol Biol. 2006 May 19;358(5):1212-20. Epub 2006 Mar 10. PMID:16564539

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