5ilb: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='5ilb' size='340' side='right' caption='[[5ilb]], [[Resolution|resolution]] 1.85Å' scene=''> | <StructureSection load='5ilb' size='340' side='right' caption='[[5ilb]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5ilb]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ILB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ILB FirstGlance]. <br> | <table><tr><td colspan='2'>[[5ilb]] is a 2 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=5ILB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ILB FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5il9|5il9]], [[5ila|5ila]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5il9|5il9]], [[5ila|5ila]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DEGP9, At5g40200, MSN9.10, MSN9.100 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=5ilb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ilb OCA], [http://pdbe.org/5ilb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ilb RCSB], [http://www.ebi.ac.uk/pdbsum/5ilb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ilb ProSAT]</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=5ilb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ilb OCA], [http://pdbe.org/5ilb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ilb RCSB], [http://www.ebi.ac.uk/pdbsum/5ilb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ilb ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/DEGP2_ARATH DEGP2_ARATH]] Serine protease that performs the primary cleavage of the photodamaged D1 protein in plant photosystem II.<ref>PMID:11179216</ref> | [[http://www.uniprot.org/uniprot/DEGP2_ARATH DEGP2_ARATH]] Serine protease that performs the primary cleavage of the photodamaged D1 protein in plant photosystem II.<ref>PMID:11179216</ref> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The high temperature requirement A (HtrA) proteases (also termed Deg proteases) play important roles in diverse organisms by regulating protein quality and quantity. One of the 16 Arabidopsis homologs, Deg9, is located in the nucleus where it modulates cytokinin- and light-mediated signalling via degrading the ARABIDOPSIS RESPONSE REGULATOR 4 (ARR4). To uncover the structural features underlying the proteolytic activity of Deg9, we determined its crystal structure. Unlike the well-established trimeric building block of HtrAs, Deg9 displays a novel octameric structure consisting of two tetrameric rings that have distinct conformations. Based on the structural architecture, we generated several mutant variants of Deg9, determined their structure and tested their proteolytic activity towards ARR4. The results of the structural and biochemical analyses allowed us to propose a model for a novel mechanism of substrate recognition and activity regulation of Deg9. In this model, protease activation of one tetramer is mediated by en-bloc reorientation of the protease domains to open an entrance for the substrate in the opposite (inactive) tetramer. This study provides the structural basis for understanding how the levels of nuclear signal components are regulated by a plant protease. | |||
The crystal structure of Deg9 reveals a novel octameric-type HtrA protease.,Ouyang M, Li X, Zhao S, Pu H, Shen J, Adam Z, Clausen T, Zhang L Nat Plants. 2017 Dec;3(12):973-982. doi: 10.1038/s41477-017-0060-2. Epub 2017 Nov, 27. PMID:29180814<ref>PMID:29180814</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5ilb" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Arath]] | |||
[[Category: Li, X Y]] | [[Category: Li, X Y]] | ||
[[Category: Liu, L]] | [[Category: Liu, L]] | ||
Revision as of 10:24, 13 December 2017
Crystal structure of protease domain of Deg2 linked with the PDZ domain of Deg9Crystal structure of protease domain of Deg2 linked with the PDZ domain of Deg9
Structural highlights
Function[DEGP2_ARATH] Serine protease that performs the primary cleavage of the photodamaged D1 protein in plant photosystem II.[1] Publication Abstract from PubMedThe high temperature requirement A (HtrA) proteases (also termed Deg proteases) play important roles in diverse organisms by regulating protein quality and quantity. One of the 16 Arabidopsis homologs, Deg9, is located in the nucleus where it modulates cytokinin- and light-mediated signalling via degrading the ARABIDOPSIS RESPONSE REGULATOR 4 (ARR4). To uncover the structural features underlying the proteolytic activity of Deg9, we determined its crystal structure. Unlike the well-established trimeric building block of HtrAs, Deg9 displays a novel octameric structure consisting of two tetrameric rings that have distinct conformations. Based on the structural architecture, we generated several mutant variants of Deg9, determined their structure and tested their proteolytic activity towards ARR4. The results of the structural and biochemical analyses allowed us to propose a model for a novel mechanism of substrate recognition and activity regulation of Deg9. In this model, protease activation of one tetramer is mediated by en-bloc reorientation of the protease domains to open an entrance for the substrate in the opposite (inactive) tetramer. This study provides the structural basis for understanding how the levels of nuclear signal components are regulated by a plant protease. The crystal structure of Deg9 reveals a novel octameric-type HtrA protease.,Ouyang M, Li X, Zhao S, Pu H, Shen J, Adam Z, Clausen T, Zhang L Nat Plants. 2017 Dec;3(12):973-982. doi: 10.1038/s41477-017-0060-2. Epub 2017 Nov, 27. PMID:29180814[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||