Crystal structures of substrate‐bound chitinase from the psychrophilic bacterium Moritella marina and its structure in solution. (1st March 2014)

• Record Type: Journal Article
• Authors: Malecki, Piotr H.; Vorgias, Constantinos E.; Petoukhov, Maxim V.; Svergun, Dmitri I.; Rypniewski, Wojciech
• Is Part Of: Acta crystallographica. Volume 70:Part 3(2014:Mar.)
• Page Start: 676
• Page End: 684
• Publication Date: 2014-03-01
• Subjects: Biomolecules -- Structure -- Periodicals; Physical biochemistry -- Periodicals; X-ray crystallography -- Periodicals; Crystallography -- Periodicals; 572
• DOI: 10.1107/S1399004713032264
• Languages: English
• ISSNs: 0907-4449

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>The four‐domain structure of chitinase 60 from <italic>Moritella marina</italic> (<italic>Mm</italic>Chi60) 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 <italic>Mm</italic>Chi60 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.</p> </abstract>