2knd: Difference between revisions
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==Psb27 structure from Synechocystis== | ==Psb27 structure from Synechocystis== | ||
<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 [ | <table><tr><td colspan='2'>[[2knd]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=2KND FirstGlance]. <br> | ||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">slr1645 ([ | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">slr1645 ([https://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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2knd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2knd OCA], [https://pdbe.org/2knd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2knd RCSB], [https://www.ebi.ac.uk/pdbsum/2knd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2knd ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://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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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Bangert, J A]] | [[Category: Bangert, J A]] | ||
[[Category: Cormann, K U]] | [[Category: Cormann, K U]] | ||
Revision as of 10:29, 14 April 2021
Psb27 structure from SynechocystisPsb27 structure from Synechocystis
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 PubMedPsb27 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 AlsoReferences
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