5wr3: Difference between revisions
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<StructureSection load='5wr3' size='340' side='right' caption='[[5wr3]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='5wr3' size='340' side='right' caption='[[5wr3]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5wr3]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WR3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WR3 FirstGlance]. <br> | <table><tr><td colspan='2'>[[5wr3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_12980 Atcc 12980]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WR3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WR3 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=NX6:N-[(BENZYLOXY)CARBONYL]-L-ASPARTIC+ACID'>NX6</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </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=NX6:N-[(BENZYLOXY)CARBONYL]-L-ASPARTIC+ACID'>NX6</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5wr6|5wr6]], [[5wr5|5wr5]], [[5wr4|5wr4]], [[5wr2|5wr2]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5wr6|5wr6]], [[5wr5|5wr5]], [[5wr4|5wr4]], [[5wr2|5wr2]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nprS, nprM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1422 ATCC 12980])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thermolysin Thermolysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.27 3.4.24.27] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thermolysin Thermolysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.27 3.4.24.27] </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=5wr3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wr3 OCA], [http://pdbe.org/5wr3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wr3 RCSB], [http://www.ebi.ac.uk/pdbsum/5wr3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wr3 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=5wr3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wr3 OCA], [http://pdbe.org/5wr3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wr3 RCSB], [http://www.ebi.ac.uk/pdbsum/5wr3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wr3 ProSAT]</span></td></tr> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Atcc 12980]] | |||
[[Category: Thermolysin]] | [[Category: Thermolysin]] | ||
[[Category: Kunishima, N]] | [[Category: Kunishima, N]] |
Revision as of 23:50, 24 January 2018
Thermolysin, SFX liganded form with water-based carrierThermolysin, SFX liganded form with water-based carrier
Structural highlights
Function[THER_GEOSE] Extracellular zinc metalloprotease.[1] Publication Abstract from PubMedSerial femtosecond crystallography (SFX) with an X-ray free-electron laser is used for the structural determination of proteins from a large number of microcrystals at room temperature. To examine the feasibility of pharmaceutical applications of SFX, a ligand-soaking experiment using thermolysin microcrystals has been performed using SFX. The results were compared with those from a conventional experiment with synchrotron radiation (SR) at 100 K. A protein-ligand complex structure was successfully obtained from an SFX experiment using microcrystals soaked with a small-molecule ligand; both oil-based and water-based crystal carriers gave essentially the same results. In a comparison of the SFX and SR structures, clear differences were observed in the unit-cell parameters, in the alternate conformation of side chains, in the degree of water coordination and in the ligand-binding mode. Protein-ligand complex structure from serial femtosecond crystallography using soaked thermolysin microcrystals and comparison with structures from synchrotron radiation.,Naitow H, Matsuura Y, Tono K, Joti Y, Kameshima T, Hatsui T, Yabashi M, Tanaka R, Tanaka T, Sugahara M, Kobayashi J, Nango E, Iwata S, Kunishima N Acta Crystallogr D Struct Biol. 2017 Aug 1;73(Pt 8):702-709. doi:, 10.1107/S2059798317008919. Epub 2017 Jul 31. PMID:28777085[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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