1gpj

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1gpj, resolution 1.95Å

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GLUTAMYL-TRNA REDUCTASE FROM METHANOPYRUS KANDLERI

Overview

Processes vital to life such as respiration and photosynthesis critically, depend on the availability of tetrapyrroles including hemes and, chlorophylls. tRNA-dependent catalysis generally is associated with, protein biosynthesis. An exception is the reduction of glutamyl-tRNA to, glutamate-1-semialdehyde by the enzyme glutamyl-tRNA reductase. This, reaction is the indispensable initiating step of tetrapyrrole biosynthesis, in plants and most prokaryotes. The crystal structure of glutamyl-tRNA, reductase from the archaeon Methanopyrus kandleri in complex with the, substrate-like inhibitor glutamycin at 1.9 A resolution reveals an, extended yet planar V-shaped dimer. The well defined interactions of the, inhibitor with the active site support a thioester-mediated reduction, process. ... [(full description)]

About this Structure

1GPJ is a [Single protein] structure of sequence from [Methanopyrus kandleri] with GMC and CIT as [ligands]. Full crystallographic information is available from [OCA].

Reference

V-shaped structure of glutamyl-tRNA reductase, the first enzyme of tRNA-dependent tetrapyrrole biosynthesis., Moser J, Schubert WD, Beier V, Bringemeier I, Jahn D, Heinz DW, EMBO J. 2001 Dec 3;20(23):6583-90. PMID:11726494

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