|
|
| (One intermediate revision not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==The crystal structure of cpFtsY from Arabidopsis thaliana== | | ==The crystal structure of cpFtsY from Arabidopsis thaliana== |
| - | <StructureSection load='3b9q' size='340' side='right' caption='[[3b9q]], [[Resolution|resolution]] 1.75Å' scene=''> | + | <StructureSection load='3b9q' size='340' side='right'caption='[[3b9q]], [[Resolution|resolution]] 1.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3b9q]] 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=3B9Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3B9Q FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3b9q]] 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=3B9Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3B9Q FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLI:MALONATE+ION'>MLI</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]] 1.75Å</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=3b9q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b9q OCA], [http://pdbe.org/3b9q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3b9q RCSB], [http://www.ebi.ac.uk/pdbsum/3b9q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3b9q ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene></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=3b9q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b9q OCA], [https://pdbe.org/3b9q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b9q RCSB], [https://www.ebi.ac.uk/pdbsum/3b9q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b9q ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CFTSY_ARATH CFTSY_ARATH]] Signal recognition particle receptor protein. Binds GTP specifically. The GTPase activity is inhibited by the N-terminus of the protein until binding to the thylakoid membrane. Activates the GTPase activity of FFC/cpSRP54 when bound to the cpSRP complex. Required for light-harvesting chlorophyll a/b-binding protein (LHCP) integration into thylakoids. Might be also functionally linked to the Sec translocation machinery.<ref>PMID:10214972</ref> <ref>PMID:10480939</ref> <ref>PMID:12105232</ref> <ref>PMID:17475780</ref> <ref>PMID:18764927</ref> <ref>PMID:19293157</ref> | + | [https://www.uniprot.org/uniprot/CFTSY_ARATH CFTSY_ARATH] Signal recognition particle receptor protein. Binds GTP specifically. The GTPase activity is inhibited by the N-terminus of the protein until binding to the thylakoid membrane. Activates the GTPase activity of FFC/cpSRP54 when bound to the cpSRP complex. Required for light-harvesting chlorophyll a/b-binding protein (LHCP) integration into thylakoids. Might be also functionally linked to the Sec translocation machinery.<ref>PMID:10214972</ref> <ref>PMID:10480939</ref> <ref>PMID:12105232</ref> <ref>PMID:17475780</ref> <ref>PMID:18764927</ref> <ref>PMID:19293157</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 32: |
Line 33: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Arath]] | + | [[Category: Arabidopsis thaliana]] |
| - | [[Category: Sinning, I]] | + | [[Category: Large Structures]] |
| - | [[Category: Stengel, K F]] | + | [[Category: Sinning I]] |
| - | [[Category: Wild, K]] | + | [[Category: Stengel KF]] |
| - | [[Category: Cpftsy]] | + | [[Category: Wild K]] |
| - | [[Category: Gtp-binding]]
| + | |
| - | [[Category: Nucleotide-binding]]
| + | |
| - | [[Category: Protein translocation]]
| + | |
| - | [[Category: Protein transport]]
| + | |
| - | [[Category: Srp receptor]]
| + | |
| Structural highlights
Function
CFTSY_ARATH Signal recognition particle receptor protein. Binds GTP specifically. The GTPase activity is inhibited by the N-terminus of the protein until binding to the thylakoid membrane. Activates the GTPase activity of FFC/cpSRP54 when bound to the cpSRP complex. Required for light-harvesting chlorophyll a/b-binding protein (LHCP) integration into thylakoids. Might be also functionally linked to the Sec translocation machinery.[1] [2] [3] [4] [5] [6]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Two GTPases in the signal recognition particle and its receptor (FtsY) regulate protein targeting to the membrane by formation of a heterodimeric complex. The activation of both GTPases in the complex is essential for protein translocation. We present the crystal structure of chloroplast FtsY (cpFtsY) at 1.75 A resolution. The comparison with FtsY structures in different nucleotide bound states shows structural changes relevant for GTPase activation and provides insights in how cpFtsY is pre-organized for complex formation with cpSRP54. The structure contains an amino-terminal amphipathic helix similar to the membrane targeting sequence of Escherichia coli FtsY. In cpFtsY this motif is extended, which might be responsible for the enhanced attachment of the protein to the thylakoid membrane.
The structure of the chloroplast signal recognition particle (SRP) receptor reveals mechanistic details of SRP GTPase activation and a conserved membrane targeting site.,Stengel KF, Holdermann I, Wild K, Sinning I FEBS Lett. 2007 Dec 11;581(29):5671-6. Epub 2007 Nov 20. PMID:18022392[7]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kogata N, Nishio K, Hirohashi T, Kikuchi S, Nakai M. Involvement of a chloroplast homologue of the signal recognition particle receptor protein, FtsY, in protein targeting to thylakoids. FEBS Lett. 1999 Mar 26;447(2-3):329-33. PMID:10214972
- ↑ 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
- ↑ Yuan J, Kight A, Goforth RL, Moore M, Peterson EC, Sakon J, Henry R. ATP stimulates signal recognition particle (SRP)/FtsY-supported protein integration in chloroplasts. J Biol Chem. 2002 Aug 30;277(35):32400-4. Epub 2002 Jun 24. PMID:12105232 doi:http://dx.doi.org/10.1074/jbc.M206192200
- ↑ Jaru-Ampornpan P, Chandrasekar S, Shan SO. Efficient interaction between two GTPases allows the chloroplast SRP pathway to bypass the requirement for an SRP RNA. Mol Biol Cell. 2007 Jul;18(7):2636-45. Epub 2007 May 2. PMID:17475780 doi:http://dx.doi.org/10.1091/mbc.E07-01-0037
- ↑ Asakura Y, Kikuchi S, Nakai M. Non-identical contributions of two membrane-bound cpSRP components, cpFtsY and Alb3, to thylakoid biogenesis. Plant J. 2008 Dec;56(6):1007-17. doi: 10.1111/j.1365-313X.2008.03659.x. Epub 2008, Aug 21. PMID:18764927 doi:http://dx.doi.org/10.1111/j.1365-313X.2008.03659.x
- ↑ Marty NJ, Rajalingam D, Kight AD, Lewis NE, Fologea D, Kumar TK, Henry RL, Goforth RL. The membrane-binding motif of the chloroplast signal recognition particle receptor (cpFtsY) regulates GTPase activity. J Biol Chem. 2009 May 29;284(22):14891-903. doi: 10.1074/jbc.M900775200. Epub, 2009 Mar 17. PMID:19293157 doi:http://dx.doi.org/10.1074/jbc.M900775200
- ↑ Stengel KF, Holdermann I, Wild K, Sinning I. The structure of the chloroplast signal recognition particle (SRP) receptor reveals mechanistic details of SRP GTPase activation and a conserved membrane targeting site. FEBS Lett. 2007 Dec 11;581(29):5671-6. Epub 2007 Nov 20. PMID:18022392 doi:10.1016/j.febslet.2007.11.024
|
