4MB5

Crystal structure of E153Q mutant of cold-adapted chitinase from Moritella complex with Nag5

Summary for 4MB5

• Entry DOI: 10.2210/pdb4mb5/pdb
• Related: 4HMC 4HMD 4HME 4MB3 4MB4
• Descriptor: Chitinase 60, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-alpha-D-glucopyranose, SODIUM ION, ... (8 entities in total)
• Functional Keywords: tim-barrel, alpha/beta-barrel ig-like, immunoglobulin like domain, chbd, chitin binding domain, chitinase, hydrolaze, low activity mutant, nag5, hydrolase, ligand binding
• Biological source: Moritella marina
• Total number of polymer chains: 1
• Total formula weight: 60408.06

Authors

Malecki, P.H.,Vorgias, C.E.,Rypniewski, W. (deposition date: 2013-08-19, release date: 2014-03-19, Last modification date: 2024-10-30)

Primary citation

Malecki, P.H.,Vorgias, C.E.,Petoukhov, M.V.,Svergun, D.I.,Rypniewski, W.
Crystal structures of substrate-bound chitinase from the psychrophilic bacterium Moritella marina and its structure in solution
Acta Crystallogr.,Sect.D, 70:676-684, 2014

PubMed 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.

PubMed: 24598737
DOI: 10.1107/S1399004713032264

Experimental method

X-RAY DIFFRACTION (1.639 Å)