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| | ==Streptomyces Erythraeus Trypsin== | | ==Streptomyces Erythraeus Trypsin== |
| - | <StructureSection load='4m7g' size='340' side='right' caption='[[4m7g]], [[Resolution|resolution]] 0.81Å' scene=''> | + | <StructureSection load='4m7g' size='340' side='right'caption='[[4m7g]], [[Resolution|resolution]] 0.81Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4m7g]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_erythreus"_(sic)_waksman_1923 "actinomyces erythreus" (sic) waksman 1923]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M7G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4M7G FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4m7g]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharopolyspora_erythraea Saccharopolyspora erythraea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M7G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4M7G 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=4m7g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m7g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4m7g RCSB], [http://www.ebi.ac.uk/pdbsum/4m7g PDBsum]</span></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]] 0.81Å</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=4m7g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m7g OCA], [https://pdbe.org/4m7g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4m7g RCSB], [https://www.ebi.ac.uk/pdbsum/4m7g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4m7g ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/TRYP_SACER TRYP_SACER] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 4m7g" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Blankenship, E]] | + | [[Category: Large Structures]] |
| - | [[Category: Lodowski, D T]] | + | [[Category: Saccharopolyspora erythraea]] |
| - | [[Category: Miyagi, M]] | + | [[Category: Blankenship E]] |
| - | [[Category: Vukoti, K]] | + | [[Category: Lodowski DT]] |
| - | [[Category: Hydrolase]] | + | [[Category: Miyagi M]] |
| - | [[Category: Serine protease]] | + | [[Category: Vukoti K]] |
| Structural highlights
Function
TRYP_SACER
Publication Abstract from PubMed
With more than 500 crystal structures determined, serine proteases make up greater than one-third of all proteases structurally examined to date, making them among the best biochemically and structurally characterized enzymes. Despite the numerous crystallographic and biochemical studies of trypsin and related serine proteases, there are still considerable shortcomings in the understanding of their catalytic mechanism. Streptomyces erythraeus trypsin (SET) does not exhibit autolysis and crystallizes readily at physiological pH; hence, it is well suited for structural studies aimed at extending the understanding of the catalytic mechanism of serine proteases. While X-ray crystallographic structures of this enzyme have been reported, no coordinates have ever been made available in the Protein Data Bank. Based on this, and observations on the extreme stability and unique properties of this particular trypsin, it was decided to crystallize it and determine its structure. Here, the first sub-angstrom resolution structure of an unmodified, unliganded trypsin crystallized at physiological pH is reported. Detailed structural analysis reveals the geometry and structural rigidity of the catalytic triad in the unoccupied active site and comparison to related serine proteases provides a context for interpretation of biochemical studies of catalytic mechanism and activity.
Conformational flexibility in the catalytic triad revealed by the high-resolution crystal structure of Streptomyces erythraeus trypsin in an unliganded state.,Blankenship E, Vukoti K, Miyagi M, Lodowski DT Acta Crystallogr D Biol Crystallogr. 2014 Mar;70(Pt 3):833-40. doi:, 10.1107/S1399004713033658. Epub 2014 Feb 22. PMID:24598752[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Blankenship E, Vukoti K, Miyagi M, Lodowski DT. Conformational flexibility in the catalytic triad revealed by the high-resolution crystal structure of Streptomyces erythraeus trypsin in an unliganded state. Acta Crystallogr D Biol Crystallogr. 2014 Mar;70(Pt 3):833-40. doi:, 10.1107/S1399004713033658. Epub 2014 Feb 22. PMID:24598752 doi:http://dx.doi.org/10.1107/S1399004713033658
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