4MB3
Crystal structure of E153Q mutant of cold-adapted chitinase from Moritella marina
Summary for 4MB3
| Entry DOI | 10.2210/pdb4mb3/pdb |
| Related | 4HMC 4HMD 4HME 4MB4 4MB5 |
| Descriptor | Chitinase 60, SODIUM ION, GLYCINE, ... (7 entities in total) |
| Functional Keywords | tim-barrel, alpha/beta-barrel ig-like, immunoglobulin like domain, chbd, chitin binding domain, nag4, chitinase, hydrolaze, low activity mutant, hydrolase |
| Biological source | Moritella marina |
| Total number of polymer chains | 1 |
| Total formula weight | 59006.11 |
| Authors | Malecki, P.H.,Vorgias, C.E.,Rypniewski, W. (deposition date: 2013-08-19, release date: 2014-03-19, Last modification date: 2024-11-13) |
| 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 Cited by 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: 24598737DOI: 10.1107/S1399004713032264 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
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