1gpj

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[[Image:1gpj.gif|left|200px]]
[[Image:1gpj.gif|left|200px]]
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{{Structure
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|PDB= 1gpj |SIZE=350|CAPTION= <scene name='initialview01'>1gpj</scene>, resolution 1.95&Aring;
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The line below this paragraph, containing "STRUCTURE_1gpj", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Cit+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=GMC:(2R,3R,4S,5S)-4-AMINO-2-[6-(DIMETHYLAMINO)-9H-PURIN-9-YL]-5-(HYDROXYMETHYL)TETRAHYDRO-3-FURANOL'>GMC</scene>
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{{STRUCTURE_1gpj| PDB=1gpj | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gpj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gpj OCA], [http://www.ebi.ac.uk/pdbsum/1gpj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gpj RCSB]</span>
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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.]]
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[[Category: glutamyl trna-reductase]]
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[[Category: Glutamyl trna-reductase]]
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[[Category: trna-dependent tetrapyrrole biosynthesis]]
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[[Category: Trna-dependent tetrapyrrole biosynthesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:51:35 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:48:46 2008''
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Revision as of 14:51, 2 May 2008

Template:STRUCTURE 1gpj

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

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