4MB3

Crystal structure of E153Q mutant of cold-adapted chitinase from Moritella marina

4MB3 の概要

• エントリーDOI: 10.2210/pdb4mb3/pdb
• 関連するPDBエントリー: 4HMC 4HMD 4HME 4MB4 4MB5
• 分子名称: Chitinase 60, SODIUM ION, GLYCINE, ... (7 entities in total)
• 機能のキーワード: tim-barrel, alpha/beta-barrel ig-like, immunoglobulin like domain, chbd, chitin binding domain, nag4, chitinase, hydrolaze, low activity mutant, hydrolase
• 由来する生物種: Moritella marina
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 59006.11

構造登録者

Malecki, P.H.,Vorgias, C.E.,Rypniewski, W. (登録日: 2013-08-19, 公開日: 2014-03-19, 最終更新日: 2024-11-13)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.55 Å)