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4yvo

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==Crystal Structure of the TPR Domain of Arabidopsis FLU (FLU-TPR)==
==Crystal Structure of the TPR Domain of Arabidopsis FLU (FLU-TPR)==
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<StructureSection load='4yvo' size='340' side='right' caption='[[4yvo]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
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<StructureSection load='4yvo' size='340' side='right'caption='[[4yvo]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4yvo]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YVO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YVO FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4yvo]] is a 1 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=4YVO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YVO FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4yvq|4yvq]]</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]] 1.45&#8491;</td></tr>
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<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=4yvo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yvo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4yvo RCSB], [http://www.ebi.ac.uk/pdbsum/4yvo 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=4yvo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yvo OCA], [https://pdbe.org/4yvo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yvo RCSB], [https://www.ebi.ac.uk/pdbsum/4yvo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yvo ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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>
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[https://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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The tetratricopeptide repeat (TPR)-containing protein FLU is a negative regulator of chlorophyll biosynthesis in plants. It directly interacts through its TPR domain with glutamyl-tRNA reductase (GluTR), the rate-limiting enzyme in the formation of delta-aminolevulinic acid (ALA). Delineation of how FLU binds to GluTR is important for understanding the molecular basis for FLU-mediated repression of synthesis of ALA, the universal tetrapyrrole precursor. Here, we characterize the FLU-GluTR interaction by solving the crystal structures of the uncomplexed TPR domain of FLU (FLU(TPR)) at 1.45-A resolution and the complex of the dimeric domain of GluTR bound to FLU(TPR) at 2.4-A resolution. Three non-canonical TPR motifs of each FLU(TPR) form a concave surface and clamp the helix bundle in the C-terminal dimeric domain of GluTR. We demonstrate that a 2:2 FLU(TPR)-GluTR complex is the functional unit for FLU-mediated GluTR regulation and suggest that the formation of the FLU-GluTR complex prevents glutamyl-tRNA, the GluTR substrate, from binding with this enzyme. These results also provide insights into the spatial regulation of ALA synthesis by the membrane-located FLU protein.
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The Non-canonical Tetratricopeptide Repeat (TPR) Domain of Fluorescent (FLU) Mediates Complex Formation with Glutamyl-tRNA Reductase.,Zhang M, Zhang F, Fang Y, Chen X, Chen Y, Zhang W, Dai HE, Lin R, Liu L J Biol Chem. 2015 Jul 10;290(28):17559-65. doi: 10.1074/jbc.M115.662981. Epub, 2015 Jun 2. PMID:26037924<ref>PMID:26037924</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4yvo" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Liu, L]]
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[[Category: Arabidopsis thaliana]]
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[[Category: Zhang, F]]
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[[Category: Large Structures]]
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[[Category: Zhang, M]]
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[[Category: Liu L]]
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[[Category: Chloroplast]]
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[[Category: Zhang F]]
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[[Category: Fluorescent protein]]
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[[Category: Zhang M]]
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[[Category: Tpr]]
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Current revision

Crystal Structure of the TPR Domain of Arabidopsis FLU (FLU-TPR)

PDB ID 4yvo

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