PDBsum entry 4mb3

Hydrolase

PDB id: 4mb3

Contents

Protein chain

528 a.a.

Ligands

GLY

MPD

IMD

Metals

_CL

_NA ×4

Waters ×909

PDB id:

4mb3

Name:

Hydrolase

Title:

Crystal structure of e153q mutant of cold-adapted chitinase from moritella marina

Structure:

Chitinase 60. Chain: a. Engineered: yes. Mutation: yes

Source:

Moritella marina. Organism_taxid: 90736. Gene: chi60. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.55Å R-factor: 0.143 R-free: 0.184

Authors:

P.H.Malecki,C.E.Vorgias,W.Rypniewski

Key ref:

P.H.Malecki et al. (2014). Crystal structures of substrate-bound chitinase from the psychrophilic bacterium Moritella marina and its structure in solution. Acta Crystallogr D Biol Crystallogr, 70, 676-684. PubMed id: 24598737 DOI: 10.1107/S1399004713032264

Date:

19-Aug-13 Release date: 19-Mar-14

Protein chain

B1VBB0  (B1VBB0_MORMI) -  chitinase from Moritella marina

Seq: 550 a.a.

Struc: 528 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.3.2.1.14 - chitinase.
• Reaction: Hydrolysis of the 1,4-beta-linkages of N-acetyl-D-glucosamine polymers of chitin.

DOI no: 10.1107/S1399004713032264

Acta Crystallogr D Biol Crystallogr 70:676-684 (2014)

PubMed id: 24598737

Crystal structures of substrate-bound chitinase from the psychrophilic bacterium Moritella marina and its structure in solution.

P.H.Malecki, C.E.Vorgias, M.V.Petoukhov, D.I.Svergun, W.Rypniewski.

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.