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1gpj
From Proteopedia
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[[Image:1gpj.gif|left|200px]] | [[Image:1gpj.gif|left|200px]] | ||
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'''GLUTAMYL-TRNA REDUCTASE FROM METHANOPYRUS KANDLERI''' | '''GLUTAMYL-TRNA REDUCTASE FROM METHANOPYRUS KANDLERI''' | ||
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[[Category: Moser, J.]] | [[Category: Moser, J.]] | ||
[[Category: Schubert, W D.]] | [[Category: Schubert, W D.]] | ||
| - | [[Category: | + | [[Category: Glutamyl trna-reductase]] |
| - | [[Category: | + | [[Category: Trna-dependent tetrapyrrole biosynthesis]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:51:35 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 14:51, 2 May 2008
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. 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 Page seeded by OCA on Fri May 2 17:51:35 2008
