Sequence and Structural Analysis of the Chitinase Insertion Domain Reveals Two Conserved Motifs Involved in Chitin-Binding 英文参考文献.docVIP

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Sequence and Structural Analysis of the Chitinase Insertion Domain Reveals Two Conserved Motifs Involved in Chitin-Binding 英文参考文献.doc

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Sequence and Structural Analysis of the Chitinase Insertion Domain Reveals Two Conserved Motifs Involved in Chitin-Binding 英文参考文献

SequenceandStructuralAnalysisoftheChitinase InsertionDomainRevealsTwoConservedMotifs InvolvedinChitin-Binding HaiLi,LesleyH.Greene* DepartmentofChemistryandBiochemistry,OldDominionUniversity,Norfolk,Virginia,UnitedStatesofAmerica Abstract Background:Chitinasesareprevalentinlifeandarefoundinspeciesincludingarchaea,bacteria,fungi,plants,andanimals. They break down chitin, which is the second most abundant carbohydrate in nature after cellulose. Hence, they are importantformaintainingabalancebetweencarbonandnitrogentrappedasinsolublechitininbiomass.Chitinasesare classifiedintotwofamilies,18and19glycosidehydrolases.Inadditiontoacatalyticdomain,whichisatriosephosphate isomerase barrel, many family 18 chitinases contain another module, i.e., chitinase insertion domain. While numerous studies focus on the biological role of the catalytic domain in chitinase activity, the function of the chitinase insertion domainisnotcompletelyunderstood.Bioinformaticsoffersanimportantavenueinwhichtofacilitateunderstandingthe roleofresidueswithinthechitinaseinsertiondomaininchitinasefunction. Results:Twenty-sevenchitinaseinsertiondomainsequences,whichincludefourexperimentallydeterminedstructuresand spanfivekingdoms,werealignedandanalyzedusingamodifiedsequenceentropyparameter.Thirty-twopositionswith conservedresidueswereidentified.Theroleoftheseconservedresidueswasexploredbyconductingastructuralanalysisof anumberofholo-enzymes.HydrogenbondingandvanderWaalscalculationsrevealedadistinctsubsetoffourconserved residuesconstitutingtwosequencemotifsthatinteractwitholigosaccharides.Theotherconservedresiduesmaybekeyto thestructure,folding,andstabilityofthisdomain. Conclusions: Sequence and structural studies of the chitinase insertion domains conducted within the framework of evolutionidentifiedfourconservedresidueswhichclearlyinteractwiththesubstrates.Furthermore,evolutionarystudies proposealinkbetweentheappearanceofthechitinaseinsertiondomainandthefunctionoffamily18chitinasesinthe subfamilyA. Ci