5che

From Proteopedia

(Difference between revisions)

Revision as of 15:35, 3 February 2016

Crystal structure of Arabidopsis glutamyl-tRNA reductase in complex with its regulatory proteins

Structural highlights

5che is a 6 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Activity:	Glutamyl-tRNA reductase, with EC number 1.2.1.70
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

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] [GLUBP_ARATH] Involved in the regulation of glutamyl-tRNA reductase (GluTR) which is important for the synthesis and distribution of 5-aminolevulinate, a precursor in heme and chlorophyll biosynthesis (PubMed:22180625). Stimulates GluTR activity and regulates glutamate-1-semialdehyde release. May play a role in heme metabolism (PubMed:24753615). Necessary for efficient photosynthetic electron transport in chloroplasts (PubMed:20657737).

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^[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
↑ Fang Y, Zhao S, Zhang F, Zhao A, Zhang W, Zhang M, Liu L. The Arabidopsis glutamyl-tRNA reductase (GluTR) forms a ternary complex with FLU and GluTR-binding protein. Sci Rep. 2016 Jan 22;6:19756. doi: 10.1038/srep19756. PMID:26794057 doi:http://dx.doi.org/10.1038/srep19756

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/5che"

@@ Line 1: / Line 1: @@
-'''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]] 3.20&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5che]] is a 6 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CHE FirstGlance]. <br>
+</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=5che FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5che OCA], [http://pdbe.org/5che PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5che RCSB], [http://www.ebi.ac.uk/pdbsum/5che PDBsum]</span></td></tr>
+</table>
+== Function ==
+[[http://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>  [[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>  [[http://www.uniprot.org/uniprot/GLUBP_ARATH GLUBP_ARATH]] Involved in the regulation of glutamyl-tRNA reductase (GluTR) which is important for the synthesis and distribution of 5-aminolevulinate, a precursor in heme and chlorophyll biosynthesis (PubMed:22180625). Stimulates GluTR activity and regulates glutamate-1-semialdehyde release. May play a role in heme metabolism (PubMed:24753615). Necessary for efficient photosynthetic electron transport in chloroplasts (PubMed:20657737).
+<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 entry 5che is ON HOLD  until Paper Publication
+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>
-Authors: Fang, Y., Liu, L.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description:
+<div class="pdbe-citations 5che" style="background-color:#fffaf0;"></div>
-[[Category: Unreleased Structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Glutamyl-tRNA reductase]]
 [[Category: Fang, Y]]
 [[Category: Liu, L]]
+[[Category: Anchor protein]]
+[[Category: Glutr]]
+[[Category: Oxidoreductase]]
+[[Category: Regulatory protein]]
+[[Category: Tertiary complex]]

5che

From Proteopedia

Revision as of 15:35, 3 February 2016

Crystal structure of Arabidopsis glutamyl-tRNA reductase in complex with its regulatory proteins

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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