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| | ==Glutamyl-tRNA Reductase from Methanopyrus kandleri== | | ==Glutamyl-tRNA Reductase from Methanopyrus kandleri== |
| - | <StructureSection load='1gpj' size='340' side='right' caption='[[1gpj]], [[Resolution|resolution]] 1.95Å' scene=''> | + | <StructureSection load='1gpj' size='340' side='right'caption='[[1gpj]], [[Resolution|resolution]] 1.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1gpj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Dsm_6324 Dsm 6324]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GPJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GPJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1gpj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanopyrus_kandleri Methanopyrus kandleri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GPJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GPJ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</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></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hemA, MK0200 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2320 DSM 6324])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</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></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamyl-tRNA_reductase Glutamyl-tRNA reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.70 1.2.1.70] </span></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gpj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gpj OCA], [https://pdbe.org/1gpj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gpj RCSB], [https://www.ebi.ac.uk/pdbsum/1gpj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gpj ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1gpj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gpj RCSB], [http://www.ebi.ac.uk/pdbsum/1gpj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1gpj ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/HEM1_METKA HEM1_METKA]] Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). In the absence of NADPH, exhibits substrate esterase activity, leading to the release of glutamate from tRNA.<ref>PMID:10521455</ref> | + | [https://www.uniprot.org/uniprot/HEM1_METKA HEM1_METKA] Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). In the absence of NADPH, exhibits substrate esterase activity, leading to the release of glutamate from tRNA.<ref>PMID:10521455</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Dsm 6324]] | + | [[Category: Large Structures]] |
| - | [[Category: Glutamyl-tRNA reductase]] | + | [[Category: Methanopyrus kandleri]] |
| - | [[Category: Beier, V]] | + | [[Category: Beier V]] |
| - | [[Category: Bringemeier, I]] | + | [[Category: Bringemeier I]] |
| - | [[Category: Heinz, D W]] | + | [[Category: Heinz DW]] |
| - | [[Category: Jahn, D]] | + | [[Category: Jahn D]] |
| - | [[Category: Moser, J]] | + | [[Category: Moser J]] |
| - | [[Category: Schubert, W D]] | + | [[Category: Schubert W-D]] |
| - | [[Category: Glutamyl trna- reductase]]
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| - | [[Category: Reductase]]
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| - | [[Category: Trna-dependent tetrapyrrole biosynthesis]]
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| Structural highlights
Function
HEM1_METKA Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). In the absence of NADPH, exhibits substrate esterase activity, leading to the release of glutamate from tRNA.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Moser J, Lorenz S, Hubschwerlen C, Rompf A, Jahn D. Methanopyrus kandleri glutamyl-tRNA reductase. J Biol Chem. 1999 Oct 22;274(43):30679-85. PMID:10521455
- ↑ Moser J, Schubert WD, Beier V, Bringemeier I, Jahn D, Heinz DW. V-shaped structure of glutamyl-tRNA reductase, the first enzyme of tRNA-dependent tetrapyrrole biosynthesis. EMBO J. 2001 Dec 3;20(23):6583-90. PMID:11726494 doi:10.1093/emboj/20.23.6583
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