1ll7: Difference between revisions
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<StructureSection load='1ll7' size='340' side='right'caption='[[1ll7]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1ll7' size='340' side='right'caption='[[1ll7]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ll7]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1ll7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cbs_120936 Cbs 120936]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LL7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LL7 FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1d2k|1d2k]], [[1ll4|1ll4]], [[1ll6|1ll6]]</div></td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1d2k|1d2k]], [[1ll4|1ll4]], [[1ll6|1ll6]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CTS1 ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CTS1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5501 CBS 120936])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Chitinase Chitinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.14 3.2.1.14] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ll7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ll7 OCA], [https://pdbe.org/1ll7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ll7 RCSB], [https://www.ebi.ac.uk/pdbsum/1ll7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ll7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Cbs 120936]] | |||
[[Category: Chitinase]] | [[Category: Chitinase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Bortone, K]] | [[Category: Bortone, K]] | ||
Revision as of 17:49, 27 October 2021
STRUCTURE OF THE E171Q MUTANT OF C. IMMITIS CHITINASE 1STRUCTURE OF THE E171Q MUTANT OF C. IMMITIS CHITINASE 1
Structural highlights
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 PubMedAllosamidin is a known inhibitor of class 18 chitinases. We show that allosamidin is a competitive inhibitor of the fungal chitinase CiX1 from Coccidioides immitis, with a K(i) of 60 nM. We report the X-ray structure of the complex and show that upon inhibitor binding the side-chain of Asp169 rotates to form an ion pair with the oxazolinium cation. The mechanism of action is thought to involve protonation of the leaving group by Glu171 and substrate assistance by the sugar acetamido moiety to form an oxazoline-like intermediate. We converted both amino acid residues to the corresponding amide and found that each mutation effectively abolishes enzyme activity. X-ray structures show the mutant enzymes retain the basic wild-type structure and that the loss of mutant activity is due to their altered chemical properties. The high affinity of allosamidin, and its similarity to the putative reaction intermediate, suggests it is a transition state analog. This helps validate our contention that the role of Asp169 is to electrostatically stabilize the reaction transition state. The structure of an allosamidin complex with the Coccidioides immitis chitinase defines a role for a second acid residue in substrate-assisted mechanism.,Bortone K, Monzingo AF, Ernst S, Robertus JD J Mol Biol. 2002 Jul 5;320(2):293-302. PMID:12079386[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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