Structure analysis of a new psychrophilic marine protease.

ABSTRACT: A new psychrophilic marine protease was found from a marine bacterium Flavobacterium YS-80 in the Chinese Yellow Sea. The protease is about 49 kD with an isoelectric point about 4.5. It consists of 480 amino acids and is homologous to a psychrophilic alkaline protease (PAP) from an Antarctic Pseudomonas species. The protein was purified from the natural bacterium fermented and crystallized. Its crystal structure (PDB ID 3U1R) was solved at 2.0 Å by Molecular Replacement using a model based on PAP, and was refined to a crystallographic R(work) of 0.16 and an R(free) of 0.21. The marine protease consists of a two domain structure with an N-terminal domain including residues 37-264 and a C-terminal domain including residues 265-480. Similar to PAP, the N-terminal domain is responsible for pro

SUBMITTER: Zhang SC 

PROVIDER: S-EPMC3223159 | biostudies-literature | 2011

REPOSITORIES: biostudies-literature