4yvo: Difference between revisions

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~~'''Unreleased structure'''~~

The ~~entry 4yvo~~ is ~~ON HOLD~~

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

== Structural highlights ==

<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>

</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.45Å</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=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>

== Function ==

[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>

== Publication Abstract from PubMed ==

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.

~~Authors:~~ Zhang, M., Zhang, F., Liu, L.

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>

~~Description~~:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

[[Category: ~~Unreleased~~ Structures]]

</div>

[[Category: Liu, L]]

[[Category: Zhang, F]]

== References ==

[[Category: Zhang, M]]

__TOC__

</StructureSection>

[[Category: Arabidopsis thaliana]]

[[Category: Large Structures]]

[[Category: Liu L]]

[[Category: Zhang F]]

[[Category: Zhang M]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 4yvo is ON HOLD
+==Crystal Structure of the TPR Domain of Arabidopsis FLU (FLU-TPR)==
+<StructureSection load='4yvo' size='340' side='right'caption='[[4yvo]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
+== Structural highlights ==
+<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>
+</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>
+<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>
+== Function ==
+[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>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-Authors: Zhang, M., Zhang, F., Liu, L.
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Liu, L]]
+<div class="pdbe-citations 4yvo" style="background-color:#fffaf0;"></div>
-[[Category: Zhang, F]]
+== References ==
-[[Category: Zhang, M]]
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Arabidopsis thaliana]]
+[[Category: Large Structures]]
+[[Category: Liu L]]
+[[Category: Zhang F]]
+[[Category: Zhang M]]