1gpj
From Proteopedia
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|PDB= 1gpj |SIZE=350|CAPTION= <scene name='initialview01'>1gpj</scene>, resolution 1.95Å | |PDB= 1gpj |SIZE=350|CAPTION= <scene name='initialview01'>1gpj</scene>, resolution 1.95Å | ||
|SITE= <scene name='pdbsite=AC1:Cit+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Cit+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=GMC:(2R,3R,4S,5S)-4-AMINO-2-[6-(DIMETHYLAMINO)-9H-PURIN-9-YL]-5-(HYDROXYMETHYL)TETRAHYDRO-3-FURANOL'>GMC | + | |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> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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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[[Category: Moser, J.]] | [[Category: Moser, J.]] | ||
[[Category: Schubert, W D.]] | [[Category: Schubert, W D.]] | ||
| - | [[Category: CIT]] | ||
| - | [[Category: GMC]] | ||
[[Category: glutamyl trna-reductase]] | [[Category: glutamyl trna-reductase]] | ||
[[Category: trna-dependent tetrapyrrole biosynthesis]] | [[Category: trna-dependent tetrapyrrole biosynthesis]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:48:46 2008'' |
Revision as of 17:48, 30 March 2008
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| , resolution 1.95Å | |||||||
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| Sites: | |||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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