3qo6
From Proteopedia
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/DEGP1_ARATH DEGP1_ARATH] Serine protease that is required at high temperature. May be involved in the degradation of damaged proteins. In vivo, can degrade beta-casein. | [https://www.uniprot.org/uniprot/DEGP1_ARATH DEGP1_ARATH] Serine protease that is required at high temperature. May be involved in the degradation of damaged proteins. In vivo, can degrade beta-casein. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Deg1 is a chloroplastic protease involved in maintaining the photosynthetic machinery. Structural and biochemical analyses reveal that the inactive Deg1 monomer is transformed into the proteolytically active hexamer at acidic pH. The change in pH is sensed by His244, which upon protonation, repositions a specific helix to trigger oligomerization. This system ensures selective activation of Deg1 during daylight, when acidification of the thylakoid lumen occurs and photosynthetic proteins are damaged. | ||
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| + | Structural adaptation of the plant protease Deg1 to repair photosystem II during light exposure.,Kley J, Schmidt B, Boyanov B, Stolt-Bergner PC, Kirk R, Ehrmann M, Knopf RR, Naveh L, Adam Z, Clausen T Nat Struct Mol Biol. 2011 Jun;18(6):728-31. Epub 2011 May 1. PMID:21532594<ref>PMID:21532594</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 3qo6" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Crystal structure analysis of the plant protease Deg1
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