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| | ==Structure of Deg protease HhoA from Synechocystis sp. PCC 6803== | | ==Structure of Deg protease HhoA from Synechocystis sp. PCC 6803== |
| - | <StructureSection load='5b6l' size='340' side='right' caption='[[5b6l]], [[Resolution|resolution]] 2.80Å' scene=''> | + | <StructureSection load='5b6l' size='340' side='right'caption='[[5b6l]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5b6l]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Escherichia_coli_bl21(de3) Escherichia coli bl21(de3)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B6L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B6L FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5b6l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21(DE3) Escherichia coli BL21(DE3)] and [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803_substr._Kazusa Synechocystis sp. PCC 6803 substr. Kazusa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B6L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B6L FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.801Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=5b6l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b6l OCA], [http://pdbe.org/5b6l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b6l RCSB], [http://www.ebi.ac.uk/pdbsum/5b6l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5b6l ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5b6l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b6l OCA], [https://pdbe.org/5b6l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b6l RCSB], [https://www.ebi.ac.uk/pdbsum/5b6l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b6l ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/HHOA_SYNY3 HHOA_SYNY3]] A putative protease, its function overlaps that of the related putative proteases HhoB and HtrA.<ref>PMID:16912048</ref> | + | [https://www.uniprot.org/uniprot/HHOA_SYNY3 HHOA_SYNY3] A putative protease, its function overlaps that of the related putative proteases HhoB and HtrA.<ref>PMID:16912048</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Dong, W]] | + | [[Category: Large Structures]] |
| - | [[Category: Liu, L]] | + | [[Category: Synechocystis sp. PCC 6803 substr. Kazusa]] |
| - | [[Category: Wang, J]] | + | [[Category: Dong W]] |
| - | [[Category: Hydrolase]] | + | [[Category: Liu L]] |
| - | [[Category: Serine protease]] | + | [[Category: Wang J]] |
| Structural highlights
Function
HHOA_SYNY3 A putative protease, its function overlaps that of the related putative proteases HhoB and HtrA.[1]
Publication Abstract from PubMed
The high temperature requirement A (HtrA) proteases are oligomeric serine proteases essential for protein quality control. HtrA homolog A (HhoA) from the photosynthetic cyanobacterium Synechocystis sp. PCC 6803 assembles into a proteolytically active hexamer. Herein, we present the crystal structure of the hexameric HhoA in complex with the copurified peptide. Our data indicate the presence of three methionines in close proximity to the peptide-binding site of the PDZ domain. Unexpectedly, we observed that a zinc ion is accommodated within the central channel formed by a HhoA trimer. However, neither calcium nor magnesium showed affinity for HhoA. The role of the zinc ion in HhoA was tested in an in vitro proteolytic assay against the nonspecific substrate beta-casein and was found to be inhibitory. Our findings provide insights into the regulation of HhoA by a redox-related mechanism involving methionine residues and by zinc ion-binding within the central channel.
Crystal structure of the zinc-bound HhoA protease from Synechocystis sp. PCC 6803.,Dong W, Wang J, Niu G, Zhao S, Liu L FEBS Lett. 2016 Oct;590(19):3435-3442. doi: 10.1002/1873-3468.12416. Epub 2016, Sep 23. PMID:27616292[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Barker M, de Vries R, Nield J, Komenda J, Nixon PJ. The deg proteases protect Synechocystis sp. PCC 6803 during heat and light stresses but are not essential for removal of damaged D1 protein during the photosystem two repair cycle. J Biol Chem. 2006 Oct 13;281(41):30347-55. Epub 2006 Aug 15. PMID:16912048 doi:http://dx.doi.org/10.1074/jbc.M601064200
- ↑ Dong W, Wang J, Niu G, Zhao S, Liu L. Crystal structure of the zinc-bound HhoA protease from Synechocystis sp. PCC 6803. FEBS Lett. 2016 Oct;590(19):3435-3442. doi: 10.1002/1873-3468.12416. Epub 2016, Sep 23. PMID:27616292 doi:http://dx.doi.org/10.1002/1873-3468.12416
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