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| | ==Structure Proteinase K at 0.98 Angstroms== | | ==Structure Proteinase K at 0.98 Angstroms== |
| - | <StructureSection load='5kxv' size='340' side='right' caption='[[5kxv]], [[Resolution|resolution]] 0.98Å' scene=''> | + | <StructureSection load='5kxv' size='340' side='right'caption='[[5kxv]], [[Resolution|resolution]] 0.98Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5kxv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Engyodontium_album Engyodontium album]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KXV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KXV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5kxv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Parengyodontium_album Parengyodontium album]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KXV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KXV FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</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]] 0.98Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5kxu|5kxu]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidase_K Peptidase K], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.64 3.4.21.64] </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=5kxv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kxv OCA], [https://pdbe.org/5kxv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kxv RCSB], [https://www.ebi.ac.uk/pdbsum/5kxv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kxv 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=5kxv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kxv OCA], [http://pdbe.org/5kxv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kxv RCSB], [http://www.ebi.ac.uk/pdbsum/5kxv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kxv ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PRTK_ENGAL PRTK_ENGAL]] Hydrolyzes keratin at aromatic and hydrophobic residues. | + | [https://www.uniprot.org/uniprot/PRTK_PARAQ PRTK_PARAQ] Hydrolyzes keratin at aromatic and hydrophobic residues. |
| | <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: Engyodontium album]] | + | [[Category: Large Structures]] |
| - | [[Category: Peptidase K]] | + | [[Category: Parengyodontium album]] |
| - | [[Category: Inoue, S]] | + | [[Category: Inoue S]] |
| - | [[Category: Masuda, T]] | + | [[Category: Masuda T]] |
| - | [[Category: Numata, K]] | + | [[Category: Numata K]] |
| - | [[Category: Sugahara, M]] | + | [[Category: Sugahara M]] |
| - | [[Category: Suzuki, M]] | + | [[Category: Suzuki M]] |
| - | [[Category: Aminolysis]]
| + | |
| - | [[Category: Catalytic triad]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Hydrolysis]]
| + | |
| - | [[Category: Serine protease]]
| + | |
| Structural highlights
Function
PRTK_PARAQ Hydrolyzes keratin at aromatic and hydrophobic residues.
Publication Abstract from PubMed
Atomic resolution structures (beyond 1.20 A) at ambient temperature, which is usually hampered by the radiation damage in synchrotron X-ray crystallography (SRX), will add to our understanding of the structure-function relationships of enzymes. Serial femtosecond crystallography (SFX) has attracted surging interest by providing a route to bypass such challenges. Yet the progress on atomic resolution analysis with SFX has been rather slow. In this report, we describe the 1.20 A resolution structure of proteinase K using 13 keV photon energy. Hydrogen atoms, water molecules, and a number of alternative side-chain conformations have been resolved. The increase in the value of B-factor in SFX suggests that the residues and water molecules adjacent to active sites were flexible and exhibited dynamic motions at specific substrate-recognition sites.
Atomic resolution structure of serine protease proteinase K at ambient temperature.,Masuda T, Suzuki M, Inoue S, Song C, Nakane T, Nango E, Tanaka R, Tono K, Joti Y, Kameshima T, Hatsui T, Yabashi M, Mikami B, Nureki O, Numata K, Iwata S, Sugahara M Sci Rep. 2017 Mar 31;7:45604. doi: 10.1038/srep45604. PMID:28361898[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Masuda T, Suzuki M, Inoue S, Song C, Nakane T, Nango E, Tanaka R, Tono K, Joti Y, Kameshima T, Hatsui T, Yabashi M, Mikami B, Nureki O, Numata K, Iwata S, Sugahara M. Atomic resolution structure of serine protease proteinase K at ambient temperature. Sci Rep. 2017 Mar 31;7:45604. doi: 10.1038/srep45604. PMID:28361898 doi:http://dx.doi.org/10.1038/srep45604
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