1gpj

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[[Image:1gpj.gif|left|200px]]<br />
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[[Image:1gpj.gif|left|200px]]<br /><applet load="1gpj" size="450" color="white" frame="true" align="right" spinBox="true"
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<applet load="1gpj" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1gpj, resolution 1.95&Aring;" />
caption="1gpj, resolution 1.95&Aring;" />
'''GLUTAMYL-TRNA REDUCTASE FROM METHANOPYRUS KANDLERI'''<br />
'''GLUTAMYL-TRNA REDUCTASE FROM METHANOPYRUS KANDLERI'''<br />
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==About this Structure==
==About this Structure==
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1GPJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanopyrus_kandleri Methanopyrus kandleri] with GMC and CIT as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GPJ OCA].
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1GPJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanopyrus_kandleri Methanopyrus kandleri] with GMC and CIT as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Cit Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GPJ OCA].
==Reference==
==Reference==
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[[Category: trna-dependent tetrapyrrole biosynthesis]]
[[Category: trna-dependent tetrapyrrole biosynthesis]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 16:16:41 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 15:29:10 2007''

Revision as of 13:19, 18 December 2007


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. Modeling the glutamyl-tRNA onto each monomer reveals an extensive, protein-tRNA interface. We furthermore propose a model whereby the large, void of glutamyl-tRNA reductase is occupied by, glutamate-1-semialdehyde-1,2-mutase, the subsequent enzyme of this, pathway, allowing for the efficient synthesis of 5-aminolevulinic acid, the common precursor of all tetrapyrroles.

About this Structure

1GPJ is a Single protein structure of sequence from Methanopyrus kandleri with GMC and CIT as ligands. Known structural/functional Site: . 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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