5che
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==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=''> | ||
| + | == Structural highlights == | ||
| + | <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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.203Å</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> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [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;"> | ||
| + | == 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<ref>PMID:26794057</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Fang | + | <div class="pdbe-citations 5che" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Arabidopsis thaliana]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Fang Y]] | ||
| + | [[Category: Liu L]] | ||
Current revision
Crystal structure of Arabidopsis glutamyl-tRNA reductase in complex with its regulatory proteins
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