دورية أكاديمية
أعرض في EDS

Structure and function of a novel GH8 endoglucanase from the bacterial cellulose synthase complex of Raoultella ornithinolytica.

التفاصيل البيبلوغرافية
العنوان: Structure and function of a novel GH8 endoglucanase from the bacterial cellulose synthase complex of Raoultella ornithinolytica.
المؤلفون: Scapin SMN; Division of Metrology Applied to Life Sciences, National Institute of Metrology, Quality and Technology, Duque de Caxias, Rio de Janeiro, Brazil., Souza FHM; Brazilian Bioethanol Science and Technology Laboratory, National Center for Research in Energy and Materials, Campinas, São Paulo, Brazil., Zanphorlin LM; Brazilian Bioethanol Science and Technology Laboratory, National Center for Research in Energy and Materials, Campinas, São Paulo, Brazil., de Almeida TS; Division of Metrology Applied to Life Sciences, National Institute of Metrology, Quality and Technology, Duque de Caxias, Rio de Janeiro, Brazil., Sade YB; Division of Metrology Applied to Life Sciences, National Institute of Metrology, Quality and Technology, Duque de Caxias, Rio de Janeiro, Brazil., Cardoso AM; Division of Metrology Applied to Life Sciences, National Institute of Metrology, Quality and Technology, Duque de Caxias, Rio de Janeiro, Brazil., Pinheiro GL; Division of Metrology Applied to Life Sciences, National Institute of Metrology, Quality and Technology, Duque de Caxias, Rio de Janeiro, Brazil., Murakami MT; Brazilian Bioethanol Science and Technology Laboratory, National Center for Research in Energy and Materials, Campinas, São Paulo, Brazil.
المصدر: PloS one [PLoS One] 2017 Apr 27; Vol. 12 (4), pp. e0176550. Date of Electronic Publication: 2017 Apr 27 (Print Publication: 2017).
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Public Library of Science Country of Publication: United States NLM ID: 101285081 Publication Model: eCollection Cited Medium: Internet ISSN: 1932-6203 (Electronic) Linking ISSN: 19326203 NLM ISO Abbreviation: PLoS One Subsets: MEDLINE
أسماء مطبوعة: Original Publication: San Francisco, CA : Public Library of Science
مواضيع طبية MeSH: Cellulase/*physiology , Enterobacteriaceae/*enzymology , Glucosyltransferases/*physiology, Cellulase/chemistry ; Cloning, Molecular ; Crystallography, X-Ray ; Enzyme Stability ; Genes, Bacterial ; Glucosyltransferases/chemistry ; Models, Molecular ; Protein Structure, Tertiary
مستخلص: Cellulose synthesis in bacteria is a complex process involving the concerted action of several enzymes whose genes are often organized in operons. This process influences many fundamental physiological aspects such as bacteria and host interaction, biofilm formation, among others. Although it might sound contradictory, the participation of cellulose-degrading enzymes is critical to this process. The presence of endoglucanases from family 8 of glycosyl hydrolases (GH8) in bacterial cellulose synthase (Bcs) complex has been described in different bacteria, including the model organism Komagataeibacter xylinus; however, their role in this process is not completely understood. In this study, we describe the biochemical characterization and three-dimensional structure of a novel GH8 member from Raoultella ornithinolytica, named AfmE1, which was previously identified by our group from the metagenomic analysis of the giant snail Achatina fulica. Our results demonstrated that AfmE1 is an endo-β-1,4-glucanase, with maximum activity in acidic to neutral pH over a wide temperature range. This enzyme cleaves cello-oligosaccharides with a degree of polymerization ≥ 5 and presents six glucosyl-binding subsites. The structural comparison of AfmE1 with other GH8 endoglucanases showed significant structural dissimilarities in the catalytic cleft, particularly in the subsite +3, which correlate with different functional mechanisms, such as the recognition of substrate molecules having different arrangements and crystallinities. Together, these findings provide new insights into molecular and structural features of evolutionarily conserved endoglucanases from the bacterial cellulose biosynthetic machinery.
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المشرفين على المادة: EC 2.4.1.- (Glucosyltransferases)
EC 2.4.1.- (cellulose synthase)
EC 3.2.1.4 (Cellulase)
تواريخ الأحداث: Date Created: 20170428 Date Completed: 20170926 Latest Revision: 20181113
رمز التحديث: 20221213
مُعرف محوري في PubMed: PMC5407803
DOI: 10.1371/journal.pone.0176550
PMID: 28448629
قاعدة البيانات: MEDLINE
الوصف
تدمد:1932-6203
DOI:10.1371/journal.pone.0176550