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Solution structure of the chitin-binding domain 1 (ChBD1) of a hyperthermophilic chitinase from Pyrococcus furiosus.

Mine S, Nakamura T, Sato T, Ikegami T, Uegaki K
J Biochem 155 115-22 (2014)
Cited: 9 times
EuropePMC logo PMID: 24272751

Abstract

A chitinase, from Pyrococcus furiosus, is a hyperthermophilic glycosidase that effectively hydrolyses both α and β crystalline chitin. This chitinase has unique structural features; it contains two catalytic domains (AD1 and AD2) and two chitin-binding domains (ChBD1 and ChBD2). We have determined the structure of ChBD1, which significantly enhances the activity of the catalytic domains, by nuclear magnetic resonance spectroscopy. The overall structure of ChBD1 had a compact and globular architecture consisting of three anti-parallel β-strands, similar to those of other proteins classified into carbohydrate-binding module (CBM) family 5. A mutagenesis experiment suggested three solvent-exposed aromatic residues (Tyr112, Trp113 and Tyr123) as the chitin-binding sites. The involvement of Tyr123 or the corresponding aromatic residues in other CBMs, has been demonstrated for the first time. This result indicates that the binding mode may be different from those of other chitin-binding domains in CBM family 5. In addition, the binding affinities of ChBD1 and ChBD2 were quite different, suggesting that the two ChBDs each play a different role in efficiently increasing the activities of AD1 and AD2.

Articles - 2rts mentioned but not cited (1)

  1. Structural and functional variation of chitin-binding domains of a lytic polysaccharide monooxygenase from Cellvibrio japonicus. Madland E, Forsberg Z, Wang Y, Lindorff-Larsen K, Niebisch A, Modregger J, Eijsink VGH, Aachmann FL, Courtade G. J Biol Chem 297 101084 (2021)


Reviews citing this publication (2)

  1. Chitin and chitinase: Role in pathogenicity, allergenicity and health. Patel S, Goyal A. Int J Biol Macromol 97 331-338 (2017)
  2. Structural Insights into the Molecular Evolution of the Archaeal Exo-β-d-Glucosaminidase. Mine S, Watanabe M. Int J Mol Sci 20 E2460 (2019)

Articles citing this publication (6)

  1. The chitin-binding domain of a GH-18 chitinase from Vibrio harveyi is crucial for chitin-chitinase interactions. Suginta W, Sirimontree P, Sritho N, Ohnuma T, Fukamizo T. Int J Biol Macromol 93 1111-1117 (2016)
  2. Expression from engineered Escherichia coli chromosome and crystallographic study of archaeal N,N'-diacetylchitobiose deacetylase. Mine S, Niiyama M, Hashimoto W, Ikegami T, Koma D, Ohmoto T, Fukuda Y, Inoue T, Abe Y, Ueda T, Morita J, Uegaki K, Nakamura T. FEBS J 281 2584-2596 (2014)
  3. Substrate recognition of N,N'-diacetylchitobiose deacetylase from Pyrococcus horikoshii. Nakamura T, Yonezawa Y, Tsuchiya Y, Niiyama M, Ida K, Oshima M, Morita J, Uegaki K. J Struct Biol 195 286-293 (2016)
  4. In silico analysis of ChtBD3 domain to find its role in bacterial pathogenesis and beyond. Patel S, Rauf A, Meher BR. Microb Pathog 110 519-526 (2017)
  5. A novel chitin-binding mode of the chitin-binding domain of chitinase A1 from Bacillus circulans WL-12 revealed by solid-state NMR. Tanaka H, Akutsu H, Yabuta I, Hara M, Sugimoto H, Ikegami T, Watanabe T, Fujiwara T. FEBS Lett 592 3173-3182 (2018)
  6. The Structure of an Archaeal β-Glucosaminidase Provides Insight into Glycoside Hydrolase Evolution. Mine S, Watanabe M, Kamachi S, Abe Y, Ueda T. J Biol Chem 292 4996-5006 (2017)


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