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| | <StructureSection load='2knd' size='340' side='right' caption='[[2knd]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | | <StructureSection load='2knd' size='340' side='right' caption='[[2knd]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2knd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KND OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KND FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2knd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aphanocapsa_sp._(strain_n-1) Aphanocapsa sp. (strain n-1)]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KND OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KND FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">slr1645 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1143 Synechocystis sp.])</td></tr> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">slr1645 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1148 Aphanocapsa sp. (strain N-1)])</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=2knd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2knd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2knd RCSB], [http://www.ebi.ac.uk/pdbsum/2knd 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=2knd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2knd OCA], [http://pdbe.org/2knd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2knd RCSB], [http://www.ebi.ac.uk/pdbsum/2knd PDBsum]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PS11_SYNY3 PS11_SYNY3]] Plays a role in the repair and/or biogenesis of the calcium-manganese-oxide cluster on the lumenal face of the thylakoid membrane. Photosystem II (PSII) complexes containing this protein are monomeric, are assembly intermediates lacking the calcium-manganese-oxide cluster and miss some of the lumenal subunits. Probably blocks binding of some of the small lumenal subunits.<ref>PMID:22031695</ref> <ref>PMID:18089572</ref> <ref>PMID:21592967</ref> <ref>PMID:22086423</ref> | + | [[http://www.uniprot.org/uniprot/PSB27_SYNY3 PSB27_SYNY3]] Plays a role in the repair and/or biogenesis of the calcium-manganese-oxide cluster on the lumenal face of the thylakoid membrane. Photosystem II (PSII) complexes containing this protein are monomeric, are assembly intermediates lacking the calcium-manganese-oxide cluster and miss some of the lumenal subunits. Probably blocks binding of some of the small lumenal subunits.<ref>PMID:18089572</ref> <ref>PMID:18834146</ref> <ref>PMID:21592967</ref> <ref>PMID:22031695</ref> <ref>PMID:22086423</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 2knd" style="background-color:#fffaf0;"></div> |
| | | | |
| | ==See Also== | | ==See Also== |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Synechocystis sp]] | |
| | [[Category: Bangert, J A]] | | [[Category: Bangert, J A]] |
| | [[Category: Cormann, K U]] | | [[Category: Cormann, K U]] |
| Structural highlights
Function
[PSB27_SYNY3] Plays a role in the repair and/or biogenesis of the calcium-manganese-oxide cluster on the lumenal face of the thylakoid membrane. Photosystem II (PSII) complexes containing this protein are monomeric, are assembly intermediates lacking the calcium-manganese-oxide cluster and miss some of the lumenal subunits. Probably blocks binding of some of the small lumenal subunits.[1] [2] [3] [4] [5]
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
Psb27 is a membrane-extrinsic subunit of Photosystem II (PSII) where it is involved in the assembly and maintenance of this large membrane protein complex that catalyzes one of the key reactions in the biosphere - the light induced oxidation of water. Here, we report for the first time the structure of Psb27 that was not observed in the previous crystal structures of PSII due to its transient binding mode. The Psb27 structure shows that the core of the protein is a right-handed four-helix bundle with an up-down-up-down topology. The electrostatic potential of the surface generated by the amphipathic helices shows a dipolar distribution which fits perfectly to the major PsbO binding site on the PSII complex. Moreover, the presented docking model could explain the function of Psb27, which prevents the binding of PsbO in order to facilitate the assembly of the Mn4Ca cluster.
Structure of Psb27 in solution: implications for transient binding to Photosystem II during biogenesis and repair.,Cormann KU, Bangert JA, Ikeuchi M, Roegner M, Stoll R, Nowaczyk MM Biochemistry. 2009 Aug 21. PMID:19697957[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Roose JL, Pakrasi HB. The Psb27 protein facilitates manganese cluster assembly in photosystem II. J Biol Chem. 2008 Feb 15;283(7):4044-50. Epub 2007 Dec 18. PMID:18089572 doi:http://dx.doi.org/10.1074/jbc.M708960200
- ↑ Bentley FK, Luo H, Dilbeck P, Burnap RL, Eaton-Rye JJ. Effects of inactivating psbM and psbT on photodamage and assembly of photosystem II in Synechocystis sp. PCC 6803. Biochemistry. 2008 Nov 4;47(44):11637-46. doi: 10.1021/bi800804h. Epub 2008 Oct, 4. PMID:18834146 doi:http://dx.doi.org/10.1021/bi800804h
- ↑ Liu H, Roose JL, Cameron JC, Pakrasi HB. A genetically tagged Psb27 protein allows purification of two consecutive photosystem II (PSII) assembly intermediates in Synechocystis 6803, a cyanobacterium. J Biol Chem. 2011 Jul 15;286(28):24865-71. doi: 10.1074/jbc.M111.246231. Epub, 2011 May 18. PMID:21592967 doi:http://dx.doi.org/10.1074/jbc.M111.246231
- ↑ Liu H, Huang RY, Chen J, Gross ML, Pakrasi HB. Psb27, a transiently associated protein, binds to the chlorophyll binding protein CP43 in photosystem II assembly intermediates. Proc Natl Acad Sci U S A. 2011 Nov 8;108(45):18536-41. doi:, 10.1073/pnas.1111597108. Epub 2011 Oct 26. PMID:22031695 doi:http://dx.doi.org/10.1073/pnas.1111597108
- ↑ Komenda J, Knoppova J, Kopecna J, Sobotka R, Halada P, Yu J, Nickelsen J, Boehm M, Nixon PJ. The Psb27 assembly factor binds to the CP43 complex of photosystem II in the cyanobacterium Synechocystis sp. PCC 6803. Plant Physiol. 2012 Jan;158(1):476-86. doi: 10.1104/pp.111.184184. Epub 2011 Nov , 15. PMID:22086423 doi:http://dx.doi.org/10.1104/pp.111.184184
- ↑ Cormann KU, Bangert JA, Ikeuchi M, Roegner M, Stoll R, Nowaczyk MM. Structure of Psb27 in solution: implications for transient binding to Photosystem II during biogenesis and repair. Biochemistry. 2009 Aug 21. PMID:19697957 doi:10.1021/bi9012726
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