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4yvq

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Revision as of 14:17, 27 April 2017

Crystal Structure of FLU-TPR in Complex with the C-terminal Region of GluTR

Structural highlights

4yvq is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	4yvo
Activity:	Glutamyl-tRNA reductase, with EC number 1.2.1.70
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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] [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.^[3] ^[4] ^[5] ^[6]

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.

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^[7]

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
↑ Meskauskiene R, Nater M, Goslings D, Kessler F, op den Camp R, Apel K. FLU: a negative regulator of chlorophyll biosynthesis in Arabidopsis thaliana. Proc Natl Acad Sci U S A. 2001 Oct 23;98(22):12826-31. Epub 2001 Oct 16. PMID:11606728 doi:http://dx.doi.org/10.1073/pnas.221252798
↑ op den Camp RG, Przybyla D, Ochsenbein C, Laloi C, Kim C, Danon A, Wagner D, Hideg E, Gobel C, Feussner I, Nater M, Apel K. Rapid induction of distinct stress responses after the release of singlet oxygen in Arabidopsis. Plant Cell. 2003 Oct;15(10):2320-32. Epub 2003 Sep 24. PMID:14508004 doi:http://dx.doi.org/10.1105/tpc.014662
↑ Goslings D, Meskauskiene R, Kim C, Lee KP, Nater M, Apel K. Concurrent interactions of heme and FLU with Glu tRNA reductase (HEMA1), the target of metabolic feedback inhibition of tetrapyrrole biosynthesis, in dark- and light-grown Arabidopsis plants. Plant J. 2004 Dec;40(6):957-67. PMID:15584960 doi:http://dx.doi.org/10.1111/j.1365-313X.2004.02262.x
↑ Przybyla D, Gobel C, Imboden A, Hamberg M, Feussner I, Apel K. Enzymatic, but not non-enzymatic, 1O2-mediated peroxidation of polyunsaturated fatty acids forms part of the EXECUTER1-dependent stress response program in the flu mutant of Arabidopsis thaliana. Plant J. 2008 Apr;54(2):236-48. doi: 10.1111/j.1365-313X.2008.03409.x. Epub 2008 , Jan 7. PMID:18182022 doi:http://dx.doi.org/10.1111/j.1365-313X.2008.03409.x
↑ Zhang M, Zhang F, Fang Y, Chen X, Chen Y, Zhang W, Dai HE, Lin R, Liu L. The Non-canonical Tetratricopeptide Repeat (TPR) Domain of Fluorescent (FLU) Mediates Complex Formation with Glutamyl-tRNA Reductase. J Biol Chem. 2015 Jul 10;290(28):17559-65. doi: 10.1074/jbc.M115.662981. Epub, 2015 Jun 2. PMID:26037924 doi:http://dx.doi.org/10.1074/jbc.M115.662981

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4yvq"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of FLU-TPR in Complex with the C-terminal Region of GluTR==
 <StructureSection load='4yvq' size='340' side='right' caption='[[4yvq]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4yvo|4yvo]]</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=4yvq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yvq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4yvq RCSB], [http://www.ebi.ac.uk/pdbsum/4yvq PDBsum]</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=4yvq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yvq OCA], [http://pdbe.org/4yvq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4yvq RCSB], [http://www.ebi.ac.uk/pdbsum/4yvq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4yvq ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4yvq" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4yvq

From Proteopedia

Revision as of 14:17, 27 April 2017

Crystal Structure of FLU-TPR in Complex with the C-terminal Region of GluTR

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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