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Article: The first crystal structures of a family 19 class IV chitinase: The enzyme from Norway spruce

TitleThe first crystal structures of a family 19 class IV chitinase: The enzyme from Norway spruce
Authors
KeywordsChitinase
Class IV
Conformational changes
Family 19
Norway spruce
Picea abies
Issue Date2009
PublisherSpringer Verlag Dordrecht. The Journal's web site is located at http://springerlink.metapress.com/openurl.asp?genre=journal&issn=0167-4412
Citation
Plant Molecular Biology, 2009, v. 71 n. 3, p. 277-289 How to Cite?
AbstractChitinases help plants defend themselves against fungal attack, and play roles in other processes, including development. The catalytic modules of most plant chitinases belong to glycoside hydrolase family 19. We report here x-ray structures of such a module from a Norway spruce enzyme, the first for any family 19 class IV chitinase. The bi-lobed structure has a wide cleft lined by conserved residues; the most interesting for catalysis are Glu113, the proton donor, and Glu122, believed to be a general base that activate a catalytic water molecule. Comparisons to class I and II enzymes show that loop deletions in the class IV proteins make the catalytic cleft shorter and wider; from modeling studies, it is predicted that only three N-acetylglucosamine-binding subsites exist in class IV. Further, the structural comparisons suggest that the family 19 enzymes become more closed on substrate binding. Attempts to solve the structure of the complete protein including the associated chitin-binding module failed, however, modeling studies based on close relatives indicate that the binding module recognizes at most three N-acetylglucosamine units. The combined results suggest that the class IV enzymes are optimized for shorter substrates than the class I and II enzymes, or alternatively, that they are better suited for action on substrates where only small regions of chitin chain are accessible. Intact spruce chitinase is shown to possess antifungal activity, which requires the binding module; removing this module had no effect on measured chitinase activity. © 2009 Springer Science+Business Media B.V.
Persistent Identifierhttp://hdl.handle.net/10722/89322
ISSN
2015 Impact Factor: 3.905
2015 SCImago Journal Rankings: 1.915
ISI Accession Number ID
Funding AgencyGrant Number
Swedish Research Council
Swedish Foundation
GLIBS
University of Hong KongORA10208034
Funding Information:

The authors would like to thank Dr. Fred Asiegbu ( Swedish University of Agricultural Sciences) for providing Heterobasidion annosum ( strain FP5), and Dr. Mark Harris (Uppsala University) for photographing the chitinase-inhibited fungal plate. The work was supported by the Swedish Research Council (VR) and the Swedish Foundation for Strategic Research via the Glycoconjugates in Biological Systems network, GLIBS (SLM), as well as by the University of Hong Kong (ORA10208034) (MLC).

References

 

DC FieldValueLanguage
dc.contributor.authorUbhayasekera, Wen_HK
dc.contributor.authorRawat, Ren_HK
dc.contributor.authorHo, SWTen_HK
dc.contributor.authorWiweger, Men_HK
dc.contributor.authorVon Arnold, Sen_HK
dc.contributor.authorChye, MLen_HK
dc.contributor.authorMowbray, SLen_HK
dc.date.accessioned2010-09-06T09:55:23Z-
dc.date.available2010-09-06T09:55:23Z-
dc.date.issued2009en_HK
dc.identifier.citationPlant Molecular Biology, 2009, v. 71 n. 3, p. 277-289en_HK
dc.identifier.issn0167-4412en_HK
dc.identifier.urihttp://hdl.handle.net/10722/89322-
dc.description.abstractChitinases help plants defend themselves against fungal attack, and play roles in other processes, including development. The catalytic modules of most plant chitinases belong to glycoside hydrolase family 19. We report here x-ray structures of such a module from a Norway spruce enzyme, the first for any family 19 class IV chitinase. The bi-lobed structure has a wide cleft lined by conserved residues; the most interesting for catalysis are Glu113, the proton donor, and Glu122, believed to be a general base that activate a catalytic water molecule. Comparisons to class I and II enzymes show that loop deletions in the class IV proteins make the catalytic cleft shorter and wider; from modeling studies, it is predicted that only three N-acetylglucosamine-binding subsites exist in class IV. Further, the structural comparisons suggest that the family 19 enzymes become more closed on substrate binding. Attempts to solve the structure of the complete protein including the associated chitin-binding module failed, however, modeling studies based on close relatives indicate that the binding module recognizes at most three N-acetylglucosamine units. The combined results suggest that the class IV enzymes are optimized for shorter substrates than the class I and II enzymes, or alternatively, that they are better suited for action on substrates where only small regions of chitin chain are accessible. Intact spruce chitinase is shown to possess antifungal activity, which requires the binding module; removing this module had no effect on measured chitinase activity. © 2009 Springer Science+Business Media B.V.en_HK
dc.languageengen_HK
dc.publisherSpringer Verlag Dordrecht. The Journal's web site is located at http://springerlink.metapress.com/openurl.asp?genre=journal&issn=0167-4412en_HK
dc.relation.ispartofPlant Molecular Biologyen_HK
dc.subjectChitinaseen_HK
dc.subjectClass IVen_HK
dc.subjectConformational changesen_HK
dc.subjectFamily 19en_HK
dc.subjectNorway spruceen_HK
dc.subjectPicea abiesen_HK
dc.titleThe first crystal structures of a family 19 class IV chitinase: The enzyme from Norway spruceen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0167-4412&volume=71&spage=277&epage=289&date=2009&atitle=The+first+crystal+structures+of+a+family+19+class+IV+chitinase:+the+enzyme+from+Norway+spruceen_HK
dc.identifier.emailChye, ML: mlchye@hkucc.hku.hken_HK
dc.identifier.authorityChye, ML=rp00687en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1007/s11103-009-9523-9en_HK
dc.identifier.pmid19629717-
dc.identifier.scopuseid_2-s2.0-69249213946en_HK
dc.identifier.hkuros165800en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-69249213946&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume71en_HK
dc.identifier.issue3en_HK
dc.identifier.spage277en_HK
dc.identifier.epage289en_HK
dc.identifier.isiWOS:000269152200006-
dc.publisher.placeNetherlandsen_HK
dc.identifier.scopusauthoridUbhayasekera, W=6506474701en_HK
dc.identifier.scopusauthoridRawat, R=8525546500en_HK
dc.identifier.scopusauthoridHo, SWT=9744286500en_HK
dc.identifier.scopusauthoridWiweger, M=55371438400en_HK
dc.identifier.scopusauthoridVon Arnold, S=7003264657en_HK
dc.identifier.scopusauthoridChye, ML=7003905460en_HK
dc.identifier.scopusauthoridMowbray, SL=7004344618en_HK
dc.identifier.citeulike5382628-

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