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| | ==Crystal structure of Arabidopsis glutamyl-tRNA reductase in complex with NADPH and GBP== | | ==Crystal structure of Arabidopsis glutamyl-tRNA reductase in complex with NADPH and GBP== |
| - | <StructureSection load='5yjl' size='340' side='right' caption='[[5yjl]], [[Resolution|resolution]] 2.70Å' scene=''> | + | <StructureSection load='5yjl' size='340' side='right'caption='[[5yjl]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5yjl]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YJL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YJL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5yjl]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YJL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YJL FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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]] 2.7Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HEMA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH]), PGR7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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=5yjl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yjl OCA], [https://pdbe.org/5yjl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yjl RCSB], [https://www.ebi.ac.uk/pdbsum/5yjl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yjl 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=5yjl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yjl OCA], [http://pdbe.org/5yjl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yjl RCSB], [http://www.ebi.ac.uk/pdbsum/5yjl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yjl ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/HEM11_ARATH HEM11_ARATH]] Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). Probably involved in the tetrapyrrole synthesis required for the chlorophyll biosynthesis.<ref>PMID:7908550</ref> <ref>PMID:12139011</ref> [[http://www.uniprot.org/uniprot/GLUBP_ARATH GLUBP_ARATH]] Involved in the regulation of glutamyl-tRNA reductase (GluTR) which is important for the synthesis and distribution of 5-aminolevulinate, a precursor in heme and chlorophyll biosynthesis (PubMed:22180625). Stimulates GluTR activity and regulates glutamate-1-semialdehyde release. May play a role in heme metabolism (PubMed:24753615). Necessary for efficient photosynthetic electron transport in chloroplasts (PubMed:20657737). | + | [https://www.uniprot.org/uniprot/HEM11_ARATH HEM11_ARATH] Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). Probably involved in the tetrapyrrole synthesis required for the chlorophyll biosynthesis.<ref>PMID:7908550</ref> <ref>PMID:12139011</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Arath]] | + | [[Category: Arabidopsis thaliana]] |
| - | [[Category: Glutamyl-tRNA reductase]] | + | [[Category: Large Structures]] |
| - | [[Category: Han, F]] | + | [[Category: Han F]] |
| - | [[Category: Zhao, A]] | + | [[Category: Zhao A]] |
| - | [[Category: Ala]]
| + | |
| - | [[Category: Gtr]]
| + | |
| - | [[Category: Photosynthesis]]
| + | |
| - | [[Category: Tetrapyrrole]]
| + | |
| Structural highlights
Function
HEM11_ARATH Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). Probably involved in the tetrapyrrole synthesis required for the chlorophyll biosynthesis.[1] [2]
Publication Abstract from PubMed
In higher plants, the tetrapyrrole biosynthesis pathway starts from the reaction catalyzed by the rate-limiting enzyme, glutamyl-tRNA(Glu) reductase (GTR). In Arabidopsis thaliana, GTR is controlled by post-transcriptional regulators such as GTR binding protein (GBP), which stimulates AtGTR activity. The NADPH-binding domain of AtGTR undergoes a substantial movement upon GBP binding. Here, we report the crystal structure of AtGTR-NADPH-GBP ternary complex. NADPH binding causes slight structural changes compared with the AtGTR-GBP binary complex, and possibly take a part of the space needed by the substrate glutamyl-tRNA(Glu). The highly reactive sulfhydryl group of the active-site residue Cys144 shows an obvious rotation, which may facilitate the hydride transfer from NADPH to the thioester intermediate to form glutamate-1-semialdehyde. Furthermore, Lys271, Lys274, Ser275, Asn278, and Gln282 of GBP participate in the interaction between AtGTR and GBP, and the stimulating effect of GBP decreased when all of these residues were mutated to Ala. When the Cys144 of AtGTR was mutated to Ser, AtGTR activity could not be detected even in the presence of GBP.
Crystal structure of Arabidopsis thaliana glutamyl-tRNA(Glu) reductase in complex with NADPH and glutamyl-tRNA(Glu) reductase binding protein.,Zhao A, Han F Photosynth Res. 2018 May 21. pii: 10.1007/s11120-018-0518-8. doi:, 10.1007/s11120-018-0518-8. PMID:29785497[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ilag LL, Kumar AM, Soll D. Light regulation of chlorophyll biosynthesis at the level of 5-aminolevulinate formation in Arabidopsis. Plant Cell. 1994 Feb;6(2):265-75. PMID:7908550 doi:http://dx.doi.org/10.1105/tpc.6.2.265
- ↑ Ujwal ML, McCormac AC, Goulding A, Kumar AM, Soll D, Terry MJ. Divergent regulation of the HEMA gene family encoding glutamyl-tRNA reductase in Arabidopsis thaliana: expression of HEMA2 is regulated by sugars, but is independent of light and plastid signalling. Plant Mol Biol. 2002 Sep;50(1):83-91. PMID:12139011
- ↑ Zhao A, Han F. Crystal structure of Arabidopsis thaliana glutamyl-tRNA(Glu) reductase in complex with NADPH and glutamyl-tRNA(Glu) reductase binding protein. Photosynth Res. 2018 May 21. pii: 10.1007/s11120-018-0518-8. doi:, 10.1007/s11120-018-0518-8. PMID:29785497 doi:http://dx.doi.org/10.1007/s11120-018-0518-8
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