4RGY

Structural and functional analysis of a low-temperature-active alkaline esterase from South China Sea marine sediment microbial metagenomic library

Summary for 4RGY

• Entry DOI: 10.2210/pdb4rgy/pdb
• Descriptor: Esterase (2 entities in total)
• Functional Keywords: hydrolase
• Biological source: uncultured bacterium FLS12
• Total number of polymer chains: 2
• Total formula weight: 60546.34

Authors

Liu, Y. (deposition date: 2014-10-01, release date: 2015-09-16, Last modification date: 2024-02-28)

Primary citation

Hu, Y.,Liu, Y.,Li, J.,Feng, Y.,Lu, N.,Zhu, B.,Xue, S.
Structural and functional analysis of a low-temperature-active alkaline esterase from South China Sea marine sediment microbial metagenomic library.
J Ind Microbiol Biotechnol, 42:1449-1461, 2015

PubMed Abstract: A low-temperature-active alkaline esterase, Est12, from a marine sediment metagenomic fosmid library was identified. Est12 prefers short- and middle-chain p-nitrophenol esters as substrate with optimum temperature and pH value of 50 °C and 9.0, respectively, and nearly 50 % of maximum activity retained at 5 °C. The hydrolysis activity of Est12 was stable at 40 °C. Ca(2+) especially activated the activity of Est12 to about 151 % of the control. DEPC and PMSF inhibited the activity of Est12 to 34 and 25 %, respectively. In addition, Est12 was more tolerable to methanol compared to other organic solvents tested. The crystal structure of Est12 at 1.39 Å resolution showed that the cap domain which is composed of an α-helix and a flexible region resulted in a relatively wide spectrum of substrate, with p-nitrophenol caproate as the preferred one. Furthermore, the flexible cap domain and the high percentage of Gly, Ser, and Met may play important roles in the adaptation of Est12 to low temperature.

PubMed: 26350078
DOI: 10.1007/s10295-015-1653-2

Experimental method

X-RAY DIFFRACTION (1.4 Å)