4n7r

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==Crystal structure of Arabidopsis glutamyl-tRNA reductase in complex with its binding protein==
==Crystal structure of Arabidopsis glutamyl-tRNA reductase in complex with its binding protein==
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<StructureSection load='4n7r' size='340' side='right' caption='[[4n7r]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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<StructureSection load='4n7r' size='340' side='right'caption='[[4n7r]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4n7r]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N7R OCA]. <br>
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<table><tr><td colspan='2'>[[4n7r]] 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=4N7R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4N7R FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.802&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4n7r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n7r OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4n7r RCSB], [http://www.ebi.ac.uk/pdbsum/4n7r PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4n7r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n7r OCA], [https://pdbe.org/4n7r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n7r RCSB], [https://www.ebi.ac.uk/pdbsum/4n7r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n7r ProSAT]</span></td></tr>
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<table>
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</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[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>
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Tetrapyrrole biosynthesis in plants, algae, and most bacteria starts from the NADPH-dependent reduction of glutamyl-tRNA by glutamyl-tRNA reductase (GluTR). The GluTR-catalyzed reaction is the rate-limiting step, and GluTR is the target of multiple posttranslational regulations, such as heme feedback inhibition, for the tetrapyrrole biosynthetic pathway. A recently identified GluTR regulator, GluTR binding protein (GluBP), has been shown to spatially organize tetrapyrrole synthesis by distributing GluTR into different suborganellar locations. Here we report the complex structure of GluTR-GluBP from Arabidopsis thaliana. The dimeric GluBP binds symmetrically to the catalytic domains of the V-shaped GluTR dimer via its C-terminal domain. A substantial conformational change of the GluTR NADPH-binding domain is observed, confirming the postulated rotation of the NADPH-binding domain for hydride transfer from NADPH to the substrate. Arg146, "guarding the door" for metabolic channeling, adopts alternative conformations, which may represent steps involved in substrate recognition and product release. A coupled enzyme assay shows that GluBP stimulates GluTR catalytic efficiency with an approximate threefold increase of the 5-aminolevulinic acid formation rate. In addition, the GluTR activity can be inhibited by heme in a concentration-dependent way regardless of the presence of GluBP. A structural alignment indicates that GluBP belongs to a heme-binding family involved in heme metabolism. We propose a catalytic mechanism model for GluTR, through which photosynthetic organisms can achieve precise regulation of tetrapyrrole biosynthesis.
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Crystal structure of Arabidopsis glutamyl-tRNA reductase in complex with its stimulator protein.,Zhao A, Fang Y, Chen X, Zhao S, Dong W, Lin Y, Gong W, Liu L Proc Natl Acad Sci U S A. 2014 May 6;111(18):6630-5. doi:, 10.1073/pnas.1400166111. Epub 2014 Apr 21. PMID:24753615<ref>PMID:24753615</ref>
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Glutamyl-tRNA reductase]]
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[[Category: Arabidopsis thaliana]]
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[[Category: Fang, Y.]]
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[[Category: Large Structures]]
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[[Category: Gong, W.]]
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[[Category: Fang Y]]
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[[Category: Lin, Y.]]
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[[Category: Gong W]]
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[[Category: Liu, L.]]
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[[Category: Lin Y]]
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[[Category: Zhao, A.]]
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[[Category: Liu L]]
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[[Category: Chloroplast]]
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[[Category: Zhao A]]
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[[Category: Nadp-binding glutamyl-trna reductase]]
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[[Category: Nadph]]
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[[Category: Oxidoreductase-protein binding complex]]
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[[Category: Reductase]]
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[[Category: Trna-glu]]
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Current revision

Crystal structure of Arabidopsis glutamyl-tRNA reductase in complex with its binding protein

PDB ID 4n7r

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