Structural insights of the enzymes from the chitin utilization locus of Flavobacterium johnsoniae

Abstract Chitin is one of the most abundant renewable organic materials found on earth. The chitin utilization locus in Flavobacterium johnsoniae, which encodes necessary proteins for complete enzymatic depolymerization of crystalline chitin, has recently been characterized but no detailed structura...

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Autores principales:	Scott Mazurkewich, Ronny Helland, Alasdair Mackenzie, Vincent G. H. Eijsink, Phillip B. Pope, Gisela Brändén, Johan Larsbrink
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/68af64a224324c0884485b7326924765
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spelling	oai:doaj.org-article:68af64a224324c0884485b73269247652021-12-02T18:50:53ZStructural insights of the enzymes from the chitin utilization locus of Flavobacterium johnsoniae10.1038/s41598-020-70749-w2045-2322https://doaj.org/article/68af64a224324c0884485b73269247652020-08-01T00:00:00Zhttps://doi.org/10.1038/s41598-020-70749-whttps://doaj.org/toc/2045-2322Abstract Chitin is one of the most abundant renewable organic materials found on earth. The chitin utilization locus in Flavobacterium johnsoniae, which encodes necessary proteins for complete enzymatic depolymerization of crystalline chitin, has recently been characterized but no detailed structural information on the enzymes was provided. Here we present protein structures of the F. johnsoniae chitobiase (FjGH20) and chitinase B (FjChiB). FjGH20 is a multi-domain enzyme with a helical domain not before observed in other chitobiases and a domain organization reminiscent of GH84 (β-N-acetylglucosaminidase) family members. The structure of FjChiB reveals that the protein lacks loops and regions associated with exo-acting activity in other chitinases and instead has a more solvent accessible substrate binding cleft, which is consistent with its endo-chitinase activity. Additionally, small angle X-ray scattering data were collected for the internal 70 kDa region that connects the N- and C-terminal chitinase domains of the unique 158 kDa multi-domain chitinase A (FjChiA). The resulting model of the molecular envelope supports bioinformatic predictions of the region comprising six domains, each with similarities to either Fn3-like or Ig-like domains. Taken together, the results provide insights into chitin utilization by F. johnsoniae and reveal structural diversity in bacterial chitin metabolism.Scott MazurkewichRonny HellandAlasdair MackenzieVincent G. H. EijsinkPhillip B. PopeGisela BrändénJohan LarsbrinkNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 10, Iss 1, Pp 1-11 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Scott Mazurkewich Ronny Helland Alasdair Mackenzie Vincent G. H. Eijsink Phillip B. Pope Gisela Brändén Johan Larsbrink Structural insights of the enzymes from the chitin utilization locus of Flavobacterium johnsoniae
description	Abstract Chitin is one of the most abundant renewable organic materials found on earth. The chitin utilization locus in Flavobacterium johnsoniae, which encodes necessary proteins for complete enzymatic depolymerization of crystalline chitin, has recently been characterized but no detailed structural information on the enzymes was provided. Here we present protein structures of the F. johnsoniae chitobiase (FjGH20) and chitinase B (FjChiB). FjGH20 is a multi-domain enzyme with a helical domain not before observed in other chitobiases and a domain organization reminiscent of GH84 (β-N-acetylglucosaminidase) family members. The structure of FjChiB reveals that the protein lacks loops and regions associated with exo-acting activity in other chitinases and instead has a more solvent accessible substrate binding cleft, which is consistent with its endo-chitinase activity. Additionally, small angle X-ray scattering data were collected for the internal 70 kDa region that connects the N- and C-terminal chitinase domains of the unique 158 kDa multi-domain chitinase A (FjChiA). The resulting model of the molecular envelope supports bioinformatic predictions of the region comprising six domains, each with similarities to either Fn3-like or Ig-like domains. Taken together, the results provide insights into chitin utilization by F. johnsoniae and reveal structural diversity in bacterial chitin metabolism.
format	article
author	Scott Mazurkewich Ronny Helland Alasdair Mackenzie Vincent G. H. Eijsink Phillip B. Pope Gisela Brändén Johan Larsbrink
author_facet	Scott Mazurkewich Ronny Helland Alasdair Mackenzie Vincent G. H. Eijsink Phillip B. Pope Gisela Brändén Johan Larsbrink
author_sort	Scott Mazurkewich
title	Structural insights of the enzymes from the chitin utilization locus of Flavobacterium johnsoniae
title_short	Structural insights of the enzymes from the chitin utilization locus of Flavobacterium johnsoniae
title_full	Structural insights of the enzymes from the chitin utilization locus of Flavobacterium johnsoniae
title_fullStr	Structural insights of the enzymes from the chitin utilization locus of Flavobacterium johnsoniae
title_full_unstemmed	Structural insights of the enzymes from the chitin utilization locus of Flavobacterium johnsoniae
title_sort	structural insights of the enzymes from the chitin utilization locus of flavobacterium johnsoniae
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/68af64a224324c0884485b7326924765
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Structural insights of the enzymes from the chitin utilization locus of Flavobacterium johnsoniae

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