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==crystal structure of the complex of subtilisin BPN' with chymotrypsin inhibitor 2 Y61A mutant== | ==crystal structure of the complex of subtilisin BPN' with chymotrypsin inhibitor 2 Y61A mutant== | ||
<StructureSection load='1to1' size='340' side='right' caption='[[1to1]], [[Resolution|resolution]] 1.68Å' scene=''> | <StructureSection load='1to1' size='340' side='right'caption='[[1to1]], [[Resolution|resolution]] 1.68Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1to1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_amyloliquifaciens"_(sic)_fukumoto_1943 "bacillus amyloliquifaciens" (sic) fukumoto 1943] and [http://en.wikipedia.org/wiki/Horvd Horvd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TO1 OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[1to1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_amyloliquifaciens"_(sic)_fukumoto_1943 "bacillus amyloliquifaciens" (sic) fukumoto 1943] and [http://en.wikipedia.org/wiki/Horvd Horvd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TO1 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1TO1 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1tm1|1tm1]], [[1tm3|1tm3]], [[1tm4|1tm4]], [[1tm5|1tm5]], [[1tm7|1tm7]], [[1tmg|1tmg]], [[1t02|1t02]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1tm1|1tm1]], [[1tm3|1tm3]], [[1tm4|1tm4]], [[1tm5|1tm5]], [[1tm7|1tm7]], [[1tmg|1tmg]], [[1t02|1t02]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">APR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1390 "Bacillus amyloliquifaciens" (sic) Fukumoto 1943])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">APR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1390 "Bacillus amyloliquifaciens" (sic) Fukumoto 1943])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1to1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1to1 OCA], [http://pdbe.org/1to1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1to1 RCSB], [http://www.ebi.ac.uk/pdbsum/1to1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1to1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| Line 16: | Line 16: | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/to/1to1_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/to/1to1_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
| Line 31: | Line 31: | ||
</div> | </div> | ||
<div class="pdbe-citations 1to1" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1to1" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Chymotrypsin Inhibitor|Chymotrypsin Inhibitor]] | |||
*[[Chymotrypsin inhibitor 3D structures|Chymotrypsin inhibitor 3D structures]] | |||
*[[Subtilisin 3D structures|Subtilisin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 36: | Line 41: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Horvd]] | [[Category: Horvd]] | ||
[[Category: Large Structures]] | |||
[[Category: Subtilisin]] | [[Category: Subtilisin]] | ||
[[Category: Koshland, D E]] | [[Category: Koshland, D E]] | ||
Revision as of 14:56, 24 December 2020
crystal structure of the complex of subtilisin BPN' with chymotrypsin inhibitor 2 Y61A mutantcrystal structure of the complex of subtilisin BPN' with chymotrypsin inhibitor 2 Y61A mutant
Structural highlights
Function[SUBT_BACAM] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. Has a high substrate specificity to fibrin.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedA series of mutants of chymotrypsin inhibitor 2 (CI2), at residues that interact with the inhibited enzyme subtilisin BPN', were studied to determine the relative importance of intermolecular contacts on either side of the scissile bond. Mutants were tested for inhibition of subtilisin, rates of hydrolysis by subtilisin, and ability to acylate subtilisin. Additionally, crystal structures of the mutant CI2 complexes with subtilisin were obtained. Ordered water molecules were found to play an important role in inhibitor recognition, and features of the crystal structures, in combination with biochemical data, support a transition-state stabilization role for the P(1) residue in subtilisin catalysis. Consistent with the proposed mechanism of inhibition, in which rapid acylation is followed by religation, leaving-group contacts with the enzyme were found to be more critical determinants of inhibition than acylating-group contacts in the mutants studied here. Binding, proteolytic, and crystallographic analyses of mutations at the protease-inhibitor interface of the subtilisin BPN'/chymotrypsin inhibitor 2 complex.,Radisky ES, Kwan G, Karen Lu CJ, Koshland DE Jr Biochemistry. 2004 Nov 2;43(43):13648-56. PMID:15504027[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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