6MVI

Apo Cel45A from Neurospora crassa OR74A

Summary for 6MVI

• Entry DOI: 10.2210/pdb6mvi/pdb
• Descriptor: Endoglucanase V (2 entities in total)
• Functional Keywords: endoglucanase v glycoside hydrolase 45 family a, hydrolase
• Biological source: Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
• Total number of polymer chains: 1
• Total formula weight: 30282.28

Authors

Kadowaki, M.A.S.,Polikarpov, I. (deposition date: 2018-10-25, release date: 2019-10-30, Last modification date: 2023-10-11)

Primary citation

Kadowaki, M.A.S.,Polikarpov, I.
Structural insights into the hydrolysis pattern and molecular dynamics simulations of GH45 subfamily a endoglucanase from Neurospora crassa OR74A.
Biochimie, 165:275-284, 2019

PubMed Abstract: Glycoside hydrolase (GH) family 45 is one of the smallest and poorly studied endoglucanase family with a broad biotechnological application ranging from treatment of textiles to conversion of complex cell wall polysaccharides into simple oligo- and monosaccharides. In a present study, GH45 cellulase from Neurospora crassa OR74A (NcCel45A) was characterized both biochemically and structurally. HPLC analysis of the hydrolytic products confirmed the endo-β(1,4) mode of action of the enzyme. Moreover, such pattern revealed that NcCel45A cannot hydrolyze efficiently oligosaccharides with a degree of polymerization smaller than six. The crystal structure of NcCel45A catalytic domain in the apo-form was determined at 1.9 Å resolution and the structure of the enzyme bound to cellobiose was solved and refined to 1.8 Å resolution. Comparative structural analyses and molecular dynamics simulations show that the enzyme dynamics is affected by substrate binding. Taken together, MD simulations and statistical coupling analysis revealed previously unknown correlation of a loop 6 with the breakdown of cellulose substrates by GH45.

PubMed: 31472178
DOI: 10.1016/j.biochi.2019.08.016

Experimental method

X-RAY DIFFRACTION (1.89 Å)