5mjw: Difference between revisions
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==Structure of Psb29 at 1.55A== | |||
<StructureSection load='5mjw' size='340' side='right' caption='[[5mjw]], [[Resolution|resolution]] 2.47Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5mjw]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MJW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MJW FirstGlance]. <br> | |||
</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=5mjw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mjw OCA], [http://pdbe.org/5mjw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mjw RCSB], [http://www.ebi.ac.uk/pdbsum/5mjw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mjw ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/THF1_THEEB THF1_THEEB]] May be involved in photosynthetic membrane biogenesis. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
One strategy for enhancing photosynthesis in crop plants is to improve their ability to repair photosystem II (PSII) in response to irreversible damage by light. Despite the pivotal role of thylakoid-embedded FtsH protease complexes in the selective degradation of PSII subunits during repair, little is known about the factors involved in regulating FtsH expression. Here we show using the cyanobacterium Synechocystis sp. PCC 6803 that the Psb29 subunit, originally identified as a minor component of His-tagged PSII preparations, physically interacts with FtsH complexes in vivo and is required for normal accumulation of the FtsH2/FtsH3 hetero-oligomeric complex involved in PSII repair. We show using X-ray crystallography that Psb29 from Thermosynechococcus elongatus has a unique fold consisting of a helical bundle and an extended C-terminal helix and contains a highly conserved region that might be involved in binding to FtsH. A similar interaction is likely to occur in Arabidopsis chloroplasts between the Psb29 homologue, termed THF1, and the FTSH2/FTSH5 complex. The direct involvement of Psb29/THF1 in FtsH accumulation helps explain why THF1 is a target during the hypersensitive response in plants induced by pathogen infection. Downregulating FtsH function and the PSII repair cycle via THF1 would contribute to the production of reactive oxygen species, the loss of chloroplast function and cell death.This article is part of the themed issue 'Enhancing photosynthesis in crop plants: targets for improvement'. | |||
Structure of Psb29/Thf1 and its association with the FtsH protease complex involved in photosystem II repair in cyanobacteria.,Bec Kova M, Yu J, Krynicka V, Kozlo A, Shao S, Konik P, Komenda J, Murray JW, Nixon PJ Philos Trans R Soc Lond B Biol Sci. 2017 Sep 26;372(1730). pii: 20160394. doi:, 10.1098/rstb.2016.0394. PMID:28808107<ref>PMID:28808107</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5mjw" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Kozlo, A]] | [[Category: Kozlo, A]] | ||
[[Category: Murray, J | [[Category: Murray, J W]] | ||
[[Category: Photosynthesis]] | |||
[[Category: Photosystem ii ftsh]] | |||
Revision as of 14:03, 24 August 2017
Structure of Psb29 at 1.55AStructure of Psb29 at 1.55A
Structural highlights
Function[THF1_THEEB] May be involved in photosynthetic membrane biogenesis. Publication Abstract from PubMedOne strategy for enhancing photosynthesis in crop plants is to improve their ability to repair photosystem II (PSII) in response to irreversible damage by light. Despite the pivotal role of thylakoid-embedded FtsH protease complexes in the selective degradation of PSII subunits during repair, little is known about the factors involved in regulating FtsH expression. Here we show using the cyanobacterium Synechocystis sp. PCC 6803 that the Psb29 subunit, originally identified as a minor component of His-tagged PSII preparations, physically interacts with FtsH complexes in vivo and is required for normal accumulation of the FtsH2/FtsH3 hetero-oligomeric complex involved in PSII repair. We show using X-ray crystallography that Psb29 from Thermosynechococcus elongatus has a unique fold consisting of a helical bundle and an extended C-terminal helix and contains a highly conserved region that might be involved in binding to FtsH. A similar interaction is likely to occur in Arabidopsis chloroplasts between the Psb29 homologue, termed THF1, and the FTSH2/FTSH5 complex. The direct involvement of Psb29/THF1 in FtsH accumulation helps explain why THF1 is a target during the hypersensitive response in plants induced by pathogen infection. Downregulating FtsH function and the PSII repair cycle via THF1 would contribute to the production of reactive oxygen species, the loss of chloroplast function and cell death.This article is part of the themed issue 'Enhancing photosynthesis in crop plants: targets for improvement'. Structure of Psb29/Thf1 and its association with the FtsH protease complex involved in photosystem II repair in cyanobacteria.,Bec Kova M, Yu J, Krynicka V, Kozlo A, Shao S, Konik P, Komenda J, Murray JW, Nixon PJ Philos Trans R Soc Lond B Biol Sci. 2017 Sep 26;372(1730). pii: 20160394. doi:, 10.1098/rstb.2016.0394. PMID:28808107[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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