|
|
| Line 1: |
Line 1: |
| | | | |
| | ==Crystal structure of Arabidopsis glutamyl-tRNA reductase in complex with its regulatory proteins== | | ==Crystal structure of Arabidopsis glutamyl-tRNA reductase in complex with its regulatory proteins== |
| - | <StructureSection load='5che' size='340' side='right' caption='[[5che]], [[Resolution|resolution]] 3.20Å' scene=''> | + | <StructureSection load='5che' size='340' side='right'caption='[[5che]], [[Resolution|resolution]] 3.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5che]] is a 6 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=5CHE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CHE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5che]] is a 6 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=5CHE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CHE FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HEMA1, HEMA, At1g58290, F19C14.9 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH]), GLUTRBP, PGR7, At3g21200, MXL8.5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH]), FLU, At3g14110, MAG2.7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr> | + | </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=5che FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5che OCA], [https://pdbe.org/5che PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5che RCSB], [https://www.ebi.ac.uk/pdbsum/5che PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5che ProSAT]</span></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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5che FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5che OCA], [http://pdbe.org/5che PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5che RCSB], [http://www.ebi.ac.uk/pdbsum/5che PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5che 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/FLU_ARATH FLU_ARATH]] Negative regulator of tetrapyrrole biosynthesis (including chlorophyll) in chloroplasts, probably via HEMA1 repression. Inhibits especially the magnesium ion Mg(2+) branch of tetrapyrrole biosynthesis, but independently of heme.<ref>PMID:11606728</ref> <ref>PMID:14508004</ref> <ref>PMID:15584960</ref> <ref>PMID:18182022</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 == |
| Line 23: |
Line 21: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Arath]] | + | [[Category: Arabidopsis thaliana]] |
| - | [[Category: Glutamyl-tRNA reductase]] | + | [[Category: Large Structures]] |
| - | [[Category: Fang, Y]] | + | [[Category: Fang Y]] |
| - | [[Category: Liu, L]] | + | [[Category: Liu L]] |
| - | [[Category: Anchor protein]]
| + | |
| - | [[Category: Glutr]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Regulatory protein]]
| + | |
| - | [[Category: Tertiary complex]]
| + | |
| 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
Tetrapyrrole biosynthesis is an essential and tightly regulated process, and glutamyl-tRNA reductase (GluTR) is a key target for multiple regulatory factors at the post-translational level. By binding to the thylakoid membrane protein FLUORESCENT (FLU) or the soluble stromal GluTR-binding protein (GBP), the activity of GluTR is down- or up-regulated. Here, we reconstructed a ternary complex composed of the C-terminal tetratricopepetide-repeat domain of FLU, GBP, and GluTR, crystallized and solved the structure of the complex at 3.2 A. The overall structure resembles the shape of merged two binary complexes as previously reported, and shows a large conformational change within GluTR. We also demonstrated that GluTR binds tightly with GBP but does not bind to GSAM under the same condition. These findings allow us to suggest a biological role of the ternary complex for the regulation of plant GluTR.
The Arabidopsis glutamyl-tRNA reductase (GluTR) forms a ternary complex with FLU and GluTR-binding protein.,Fang Y, Zhao S, Zhang F, Zhao A, Zhang W, Zhang M, Liu L Sci Rep. 2016 Jan 22;6:19756. doi: 10.1038/srep19756. PMID:26794057[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
- ↑ Fang Y, Zhao S, Zhang F, Zhao A, Zhang W, Zhang M, Liu L. The Arabidopsis glutamyl-tRNA reductase (GluTR) forms a ternary complex with FLU and GluTR-binding protein. Sci Rep. 2016 Jan 22;6:19756. doi: 10.1038/srep19756. PMID:26794057 doi:http://dx.doi.org/10.1038/srep19756
|
