1ogb: Difference between revisions
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<StructureSection load='1ogb' size='340' side='right'caption='[[1ogb]], [[Resolution|resolution]] 1.85Å' scene=''> | <StructureSection load='1ogb' size='340' side='right'caption='[[1ogb]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ogb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1ogb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OGB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OGB FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1ogb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ogb OCA], [https://pdbe.org/1ogb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ogb RCSB], [https://www.ebi.ac.uk/pdbsum/1ogb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ogb ProSAT]</span></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=1ogb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ogb OCA], [https://pdbe.org/1ogb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ogb RCSB], [https://www.ebi.ac.uk/pdbsum/1ogb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ogb ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/CHIB_SERMA CHIB_SERMA] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Serratia marcescens]] | ||
[[Category: Eijsink | [[Category: Eijsink VGH]] | ||
[[Category: Houston | [[Category: Houston DR]] | ||
[[Category: Peter | [[Category: Peter MG]] | ||
[[Category: Rao | [[Category: Rao FV]] | ||
[[Category: Synstad | [[Category: Synstad B]] | ||
[[Category: Vaaje-Kolstad | [[Category: Vaaje-Kolstad G]] | ||
[[Category: | [[Category: Van Aalten DMF]] | ||
Revision as of 15:39, 13 December 2023
Chitinase b from Serratia marcescens mutant D142NChitinase b from Serratia marcescens mutant D142N
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCatalysis by ChiB, a family 18 chitinase from Serratia marcescens, involves a conformational change of Asp142 which is part of a characteristic D(140)XD(142)XE(144) sequence motif. In the free enzyme Asp142 points towards Asp140, whereas it rotates towards the catalytic acid, Glu144, upon ligand binding. Mutation of Asp142 to Asn reduced k(cat) and affinity for allosamidin, a competitive inhibitor. The X-ray structure of the D142N mutant showed that Asn142 points towards Glu144 in the absence of a ligand. The active site also showed other structural adjustments (Tyr10, Ser93) that had previously been observed in the wild-type enzyme upon substrate binding. The X-ray structure of a complex of D142N with allosamidin, a pseudotrisaccharide competitive inhibitor, was essentially identical to that of the wild-type enzyme in complex with the same compound. Thus, the reduced allosamidin affinity in the mutant is not caused by structural changes but solely by the loss of electrostatic interactions with Asp142. The importance of electrostatics was further confirmed by the pH dependence of catalysis and allosamidin inhibition. The pH-dependent apparent affinities for allosamidin were not correlated with k(cat), indicating that it is probably better to view the inhibitor as a mimic of the oxazolinium ion reaction intermediate than as a transition state analogue. Structure of the D142N mutant of the family 18 chitinase ChiB from Serratia marcescens and its complex with allosamidin.,Vaaje-Kolstad G, Houston DR, Rao FV, Peter MG, Synstad B, van Aalten DM, Eijsink VG Biochim Biophys Acta. 2004 Jan 14;1696(1):103-11. PMID:14726210[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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