Structural relationships in the lysozyme superfamily: significant evidence for glycoside hydrolase signature motifs.

<h4>Background</h4>Chitin is a polysaccharide that forms the hard, outer shell of arthropods and the cell walls of fungi and some algae. Peptidoglycan is a polymer of sugars and amino acids constituting the cell walls of most bacteria. Enzymes that are able to hydrolyze these cell membra...

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Autores principales:	Alexandre Wohlkönig, Joëlle Huet, Yvan Looze, René Wintjens
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2010
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/1f198c5555784348b3466f8fdf58ef81
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spelling	oai:doaj.org-article:1f198c5555784348b3466f8fdf58ef812021-11-18T07:37:01ZStructural relationships in the lysozyme superfamily: significant evidence for glycoside hydrolase signature motifs.1932-620310.1371/journal.pone.0015388https://doaj.org/article/1f198c5555784348b3466f8fdf58ef812010-11-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21085702/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203<h4>Background</h4>Chitin is a polysaccharide that forms the hard, outer shell of arthropods and the cell walls of fungi and some algae. Peptidoglycan is a polymer of sugars and amino acids constituting the cell walls of most bacteria. Enzymes that are able to hydrolyze these cell membrane polymers generally play important roles for protecting plants and animals against infection with insects and pathogens. A particular group of such glycoside hydrolase enzymes share some common features in their three-dimensional structure and in their molecular mechanism, forming the lysozyme superfamily.<h4>Results</h4>Besides having a similar fold, all known catalytic domains of glycoside hydrolase proteins of lysozyme superfamily (families and subfamilies GH19, GH22, GH23, GH24 and GH46) share in common two structural elements: the central helix of the all-α domain, which invariably contains the catalytic glutamate residue acting as general-acid catalyst, and a β-hairpin pointed towards the substrate binding cleft. The invariant β-hairpin structure is interestingly found to display the highest amino acid conservation in aligned sequences of a given family, thereby allowing to define signature motifs for each GH family. Most of such signature motifs are found to have promising performances for searching sequence databases. Our structural analysis further indicates that the GH motifs participate in enzymatic catalysis essentially by containing the catalytic water positioning residue of inverting mechanism.<h4>Conclusions</h4>The seven families and subfamilies of the lysozyme superfamily all have in common a β-hairpin structure which displays a family-specific sequence motif. These GH β-hairpin motifs contain potentially important residues for the catalytic activity, thereby suggesting the participation of the GH motif to catalysis and also revealing a common catalytic scheme utilized by enzymes of the lysozyme superfamily.Alexandre WohlkönigJoëlle HuetYvan LoozeRené WintjensPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 5, Iss 11, p e15388 (2010)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Alexandre Wohlkönig Joëlle Huet Yvan Looze René Wintjens Structural relationships in the lysozyme superfamily: significant evidence for glycoside hydrolase signature motifs.
description	<h4>Background</h4>Chitin is a polysaccharide that forms the hard, outer shell of arthropods and the cell walls of fungi and some algae. Peptidoglycan is a polymer of sugars and amino acids constituting the cell walls of most bacteria. Enzymes that are able to hydrolyze these cell membrane polymers generally play important roles for protecting plants and animals against infection with insects and pathogens. A particular group of such glycoside hydrolase enzymes share some common features in their three-dimensional structure and in their molecular mechanism, forming the lysozyme superfamily.<h4>Results</h4>Besides having a similar fold, all known catalytic domains of glycoside hydrolase proteins of lysozyme superfamily (families and subfamilies GH19, GH22, GH23, GH24 and GH46) share in common two structural elements: the central helix of the all-α domain, which invariably contains the catalytic glutamate residue acting as general-acid catalyst, and a β-hairpin pointed towards the substrate binding cleft. The invariant β-hairpin structure is interestingly found to display the highest amino acid conservation in aligned sequences of a given family, thereby allowing to define signature motifs for each GH family. Most of such signature motifs are found to have promising performances for searching sequence databases. Our structural analysis further indicates that the GH motifs participate in enzymatic catalysis essentially by containing the catalytic water positioning residue of inverting mechanism.<h4>Conclusions</h4>The seven families and subfamilies of the lysozyme superfamily all have in common a β-hairpin structure which displays a family-specific sequence motif. These GH β-hairpin motifs contain potentially important residues for the catalytic activity, thereby suggesting the participation of the GH motif to catalysis and also revealing a common catalytic scheme utilized by enzymes of the lysozyme superfamily.
format	article
author	Alexandre Wohlkönig Joëlle Huet Yvan Looze René Wintjens
author_facet	Alexandre Wohlkönig Joëlle Huet Yvan Looze René Wintjens
author_sort	Alexandre Wohlkönig
title	Structural relationships in the lysozyme superfamily: significant evidence for glycoside hydrolase signature motifs.
title_short	Structural relationships in the lysozyme superfamily: significant evidence for glycoside hydrolase signature motifs.
title_full	Structural relationships in the lysozyme superfamily: significant evidence for glycoside hydrolase signature motifs.
title_fullStr	Structural relationships in the lysozyme superfamily: significant evidence for glycoside hydrolase signature motifs.
title_full_unstemmed	Structural relationships in the lysozyme superfamily: significant evidence for glycoside hydrolase signature motifs.
title_sort	structural relationships in the lysozyme superfamily: significant evidence for glycoside hydrolase signature motifs.
publisher	Public Library of Science (PLoS)
publishDate	2010
url	https://doaj.org/article/1f198c5555784348b3466f8fdf58ef81
work_keys_str_mv	AT alexandrewohlkonig structuralrelationshipsinthelysozymesuperfamilysignificantevidenceforglycosidehydrolasesignaturemotifs AT joellehuet structuralrelationshipsinthelysozymesuperfamilysignificantevidenceforglycosidehydrolasesignaturemotifs AT yvanlooze structuralrelationshipsinthelysozymesuperfamilysignificantevidenceforglycosidehydrolasesignaturemotifs AT renewintjens structuralrelationshipsinthelysozymesuperfamilysignificantevidenceforglycosidehydrolasesignaturemotifs
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Structural relationships in the lysozyme superfamily: significant evidence for glycoside hydrolase signature motifs.

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