@article{3088411,
    title = "Crystal structures of substrate-bound chitinase from the psychrophilic bacterium Moritella marina and its structure in solution",
    author = "Malecki, P.H. and Vorgias, C.E. and Petoukhov, M.V. and Svergun, D.I. and Rypniewski, W.",
    journal = "Acta Crystallographica Section D: Biological Crystallography",
    year = "2014",
    volume = "70",
    number = "3",
    pages = "676-684",
    issn = "0907-4449, 1399-0047",
    doi = "10.1107/S1399004713032264",
    keywords = "chitin;  chitinase;  chitotetrose;  ligand;  oligosaccharide, article;  chemistry;  chitin-binding domain;  enzyme specificity;  enzymology;  flexibility;  genetics;  hinge regions;  Ig-like domain;  ligand binding;  metabolism;  Moritella;  multi-domain;  point mutation;  protein conformation;  protein multimerization;  psychrophilic;  SAXS;  small angle scattering;  solution and solubility;  TIM β/α-barrel;  X ray crystallography;  X ray diffraction, chitin;  chitin-binding domain;  chitinase;  flexibility;  hinge regions;  Ig-like domain;  ligand binding;  multi-domain;  psychrophilic;  SAXS;  TIM β/α-barrel, Chitinase;  Crystallography, X-Ray;  Ligands;  Moritella;  Oligosaccharides;  Point Mutation;  Protein Conformation;  Protein Multimerization;  Scattering, Small Angle;  Solutions;  Substrate Specificity;  X-Ray Diffraction",
    abstract = "The four-domain structure of chitinase 60 from Moritella marina (MmChi60) is outstanding in its complexity. Many glycoside hydrolases, such as chitinases and cellulases, have multi-domain structures, but only a few have been solved. The flexibility of the hinge regions between the domains apparently makes these proteins difficult to crystallize. The analysis of an active-site mutant of MmChi60 in an unliganded form and in complex with the substrates NAG4 and NAG5 revealed significant differences in the substrate-binding site compared with the previously determined complexes of most studied chitinases. A SAXS experiment demonstrated that in addition to the elongated state found in the crystal, the protein can adapt other conformations in solution ranging from fully extended to compact. © 2014 International Union of Crystallography."
}