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5e4x

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Crystal structure of cpSRP43 chromodomain 3

Structural highlights

5e4x is a 1 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.75Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SR43C_ARATH Component of the chloroplast signal recognition particle pathway. Required for post-translational targeting of proteins into the tylakoid membrane but seems to be dispensable for co-translational targeting with a translating ribosome present. May be able to function independently of cpFTSY and FFC/cpSRP54 in targeting LHCPs to the thylakoids. Acts as a highly specific chaperone for LHCPs, preventing aggregation and being able to dissolve aggregates.^[1] ^[2] ^[3] ^[4] ^[5]

Publication Abstract from PubMed

Canonical membrane protein biogenesis requires co-translational delivery of ribosome-associated proteins to the Sec translocase and depends on the signal recognition particle (SRP) and its receptor (SR). In contrast, high-throughput delivery of abundant light-harvesting chlorophyll a,b-binding proteins (LHCPs) in chloroplasts to the Alb3 insertase occurs post-translationally via a soluble transit complex including the cpSRP43/cpSRP54 heterodimer (cpSRP). Here we describe the molecular mechanisms of tethering cpSRP to the Alb3 insertase by specific interaction of cpSRP43 chromodomain 3 with a linear motif in the Alb3 C-terminal tail. Combining NMR spectroscopy, X-ray crystallography and biochemical analyses, we dissect the structural basis for selectivity of chromodomains 2 and 3 for their respective ligands cpSRP54 and Alb3, respectively. Negative cooperativity in ligand binding can be explained by dynamics in the chromodomain interface. Our study provides a model for membrane recruitment of the transit complex and may serve as a prototype for a functional gain by the tandem arrangement of chromodomains.

Structural basis for cpSRP43 chromodomain selectivity and dynamics in Alb3 insertase interaction.,Horn A, Hennig J, Ahmed YL, Stier G, Wild K, Sattler M, Sinning I Nat Commun. 2015 Nov 16;6:8875. doi: 10.1038/ncomms9875. PMID:26568381^[6]

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

References

↑ Klimyuk VI, Persello-Cartieaux F, Havaux M, Contard-David P, Schuenemann D, Meiherhoff K, Gouet P, Jones JD, Hoffman NE, Nussaume L. A chromodomain protein encoded by the arabidopsis CAO gene is a plant-specific component of the chloroplast signal recognition particle pathway that is involved in LHCP targeting. Plant Cell. 1999 Jan;11(1):87-99. PMID:9878634
↑ Tu CJ, Schuenemann D, Hoffman NE. Chloroplast FtsY, chloroplast signal recognition particle, and GTP are required to reconstitute the soluble phase of light-harvesting chlorophyll protein transport into thylakoid membranes. J Biol Chem. 1999 Sep 17;274(38):27219-24. PMID:10480939
↑ Goforth RL, Peterson EC, Yuan J, Moore MJ, Kight AD, Lohse MB, Sakon J, Henry RL. Regulation of the GTPase cycle in post-translational signal recognition particle-based protein targeting involves cpSRP43. J Biol Chem. 2004 Oct 8;279(41):43077-84. Epub 2004 Aug 2. PMID:15292240 doi:http://dx.doi.org/10.1074/jbc.M401600200
↑ Tzvetkova-Chevolleau T, Hutin C, Noel LD, Goforth R, Carde JP, Caffarri S, Sinning I, Groves M, Teulon JM, Hoffman NE, Henry R, Havaux M, Nussaume L. Canonical signal recognition particle components can be bypassed for posttranslational protein targeting in chloroplasts. Plant Cell. 2007 May;19(5):1635-48. Epub 2007 May 18. PMID:17513500 doi:http://dx.doi.org/10.1105/tpc.106.048959
↑ Falk S, Sinning I. cpSRP43 is a novel chaperone specific for light-harvesting chlorophyll a,b-binding proteins. J Biol Chem. 2010 Jul 9;285(28):21655-61. doi: 10.1074/jbc.C110.132746. Epub 2010, May 24. PMID:20498370 doi:http://dx.doi.org/10.1074/jbc.C110.132746
↑ Horn A, Hennig J, Ahmed YL, Stier G, Wild K, Sattler M, Sinning I. Structural basis for cpSRP43 chromodomain selectivity and dynamics in Alb3 insertase interaction. Nat Commun. 2015 Nov 16;6:8875. doi: 10.1038/ncomms9875. PMID:26568381 doi:http://dx.doi.org/10.1038/ncomms9875

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5e4x"

@@ Line 3: / Line 3: @@
 <StructureSection load='5e4x' size='340' side='right'caption='[[5e4x]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5e4x]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E4X OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5E4X FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5e4x]] 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=5E4X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5E4X FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.75&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CAO, CPSRP43, At2g47450, T30B22.25 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5e4x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e4x OCA], [http://pdbe.org/5e4x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e4x RCSB], [http://www.ebi.ac.uk/pdbsum/5e4x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e4x ProSAT]</span></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=5e4x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e4x OCA], [https://pdbe.org/5e4x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5e4x RCSB], [https://www.ebi.ac.uk/pdbsum/5e4x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5e4x ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/SR43C_ARATH SR43C_ARATH]] Component of the chloroplast signal recognition particle pathway. Required for post-translational targeting of proteins into the tylakoid membrane but seems to be dispensable for co-translational targeting with a translating ribosome present. May be able to function independently of cpFTSY and FFC/cpSRP54 in targeting LHCPs to the thylakoids. Acts as a highly specific chaperone for LHCPs, preventing aggregation and being able to dissolve aggregates.<ref>PMID:9878634</ref> <ref>PMID:10480939</ref> <ref>PMID:15292240</ref> <ref>PMID:17513500</ref> <ref>PMID:20498370</ref>
+[https://www.uniprot.org/uniprot/SR43C_ARATH SR43C_ARATH] Component of the chloroplast signal recognition particle pathway. Required for post-translational targeting of proteins into the tylakoid membrane but seems to be dispensable for co-translational targeting with a translating ribosome present. May be able to function independently of cpFTSY and FFC/cpSRP54 in targeting LHCPs to the thylakoids. Acts as a highly specific chaperone for LHCPs, preventing aggregation and being able to dissolve aggregates.<ref>PMID:9878634</ref> <ref>PMID:10480939</ref> <ref>PMID:15292240</ref> <ref>PMID:17513500</ref> <ref>PMID:20498370</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 21: @@
 ==See Also==
-*[[Signal recognition particle protein|Signal recognition particle protein]]
+*[[Signal recognition particle 3D structures|Signal recognition particle 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Arath]]
+[[Category: Arabidopsis thaliana]]
 [[Category: Large Structures]]
-[[Category: Ahmed, Y L]]
+[[Category: Ahmed YL]]
-[[Category: Horn, A]]
+[[Category: Horn A]]
-[[Category: Sinning, I]]
+[[Category: Sinning I]]
-[[Category: Wild, K]]
+[[Category: Wild K]]
-[[Category: Chloroplast]]
-[[Category: Chromodomain 3]]
-[[Category: Cpsrp43]]
-[[Category: Signal recognition particle]]
-[[Category: Transport protein]]

5e4x

From Proteopedia

Current revision

Crystal structure of cpSRP43 chromodomain 3

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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