1ur9: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ur9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UR9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UR9 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1ur9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UR9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UR9 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDL:2-ACETAMIDO-2-DEOXY-D-GLUCONO-1,5-LACTONE'>GDL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PHJ:N-[(AMINOOXY)CARBONYL]-N-PHENYLAMINE'>PHJ</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDL:2-ACETAMIDO-2-DEOXY-D-GLUCONO-1,5-LACTONE'>GDL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PHJ:N-[(AMINOOXY)CARBONYL]-N-PHENYLAMINE'>PHJ</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1e15|1e15]], [[1e6n|1e6n]], [[1e6p|1e6p]], [[1e6r|1e6r]], [[1e6z|1e6z]], [[1goi|1goi]], [[1gpf|1gpf]], [[1ogb|1ogb]], [[1ur8|1ur8]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1e15|1e15]], [[1e6n|1e6n]], [[1e6p|1e6p]], [[1e6r|1e6r]], [[1e6z|1e6z]], [[1goi|1goi]], [[1gpf|1gpf]], [[1ogb|1ogb]], [[1ur8|1ur8]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chitinase Chitinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.14 3.2.1.14] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chitinase Chitinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.14 3.2.1.14] </span></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ur9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ur9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ur9 RCSB], [http://www.ebi.ac.uk/pdbsum/1ur9 PDBsum]</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=1ur9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ur9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ur9 RCSB], [http://www.ebi.ac.uk/pdbsum/1ur9 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Chitinase]] | [[Category: Chitinase]] | ||
[[Category: Serratia marcescens]] | [[Category: Serratia marcescens]] | ||
[[Category: Aalten, D M.F Van | [[Category: Aalten, D M.F Van]] | ||
[[Category: Eijsink, V G.H | [[Category: Eijsink, V G.H]] | ||
[[Category: Houston, D R | [[Category: Houston, D R]] | ||
[[Category: Netter, C | [[Category: Netter, C]] | ||
[[Category: Peter, M G | [[Category: Peter, M G]] | ||
[[Category: Synstad, B | [[Category: Synstad, B]] | ||
[[Category: Vaaje-Kolstad, G | [[Category: Vaaje-Kolstad, G]] | ||
[[Category: Vasella, A | [[Category: Vasella, A]] | ||
[[Category: Westereng, B | [[Category: Westereng, B]] | ||
[[Category: Chitin degradation]] | [[Category: Chitin degradation]] | ||
[[Category: Glycosidase]] | [[Category: Glycosidase]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Inhibition]] | [[Category: Inhibition]] | ||
[[Category: Lactone]] | [[Category: Lactone]] | ||
Revision as of 16:44, 6 January 2015
INTERACTIONS OF A FAMILY 18 CHITINASE WITH THE DESIGNED INHIBITOR HM508, AND ITS DEGRADATION PRODUCT, CHITOBIONO-DELTA-LACTONEINTERACTIONS OF A FAMILY 18 CHITINASE WITH THE DESIGNED INHIBITOR HM508, AND ITS DEGRADATION PRODUCT, CHITOBIONO-DELTA-LACTONE
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 PubMedWe describe enzymological and structural analyses of the interaction between the family 18 chitinase ChiB from Serratia marcescens and the designed inhibitor N,N'-diacetylchitobionoxime-N-phenylcarbamate (HM508). HM508 acts as a competitive inhibitor of this enzyme with a K(i) in the 50 microM range. Active site mutants of ChiB show K(i) values ranging from 1 to 200 microM, providing insight into some of the interactions that determine inhibitor affinity. Interestingly, the wild type enzyme slowly degrades HM508, but the inhibitor is essentially stable in the presence of the moderately active D142N mutant of ChiB. The crystal structure of the D142N-HM508 complex revealed that the two sugar moieties bind to the -2 and -1 subsites, whereas the phenyl group interacts with aromatic side chains that line the +1 and +2 subsites. Enzymatic degradation of HM508, as well as a Trp --> Ala mutation in the +2 subsite of ChiB, led to reduced affinity for the inhibitor, showing that interactions between the phenyl group and the enzyme contribute to binding. Interestingly, a complex of enzymatically degraded HM508 with the wild type enzyme showed a chitobiono-delta-lactone bound in the -2 and -1 subsites, despite the fact that the equilibrium between the lactone and the hydroxy acid forms in solution lies far toward the latter. This shows that the active site preferentially binds the (4)E conformation of the -1 sugar, which resembles the proposed transition state of the reaction. Interactions of a family 18 chitinase with the designed inhibitor HM508 and its degradation product, chitobiono-delta-lactone.,Vaaje-Kolstad G, Vasella A, Peter MG, Netter C, Houston DR, Westereng B, Synstad B, Eijsink VG, van Aalten DM J Biol Chem. 2004 Jan 30;279(5):3612-9. Epub 2003 Nov 3. PMID:14597613[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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