3QR3

Crystal Structure of Cel5A (EG2) from Hypocrea jecorina (Trichoderma reesei)

Summary for 3QR3

• Entry DOI: 10.2210/pdb3qr3/pdb
• Descriptor: Endoglucanase EG-II, SULFATE ION, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: tim barrel, endoglucanase, hydrolase
• Biological source: Hypocrea jecorina (Hypocrea jecorina)
• Total number of polymer chains: 2
• Total formula weight: 74620.16

Authors

Lee, T.M.,Farrow, M.F.,Kaiser, J.T.,Arnold, F.H.,Mayo, S.L. (deposition date: 2011-02-16, release date: 2011-11-02, Last modification date: 2024-10-16)

Primary citation

Lee, T.M.,Farrow, M.F.,Arnold, F.H.,Mayo, S.L.
A structural study of Hypocrea jecorina Cel5A.
Protein Sci., 20:1935-1940, 2011

PubMed Abstract: Interest in generating lignocellulosic biofuels through enzymatic hydrolysis continues to rise as nonrenewable fossil fuels are depleted. The high cost of producing cellulases, hydrolytic enzymes that cleave cellulose into fermentable sugars, currently hinders economically viable biofuel production. Here, we report the crystal structure of a prevalent endoglucanase in the biofuels industry, Cel5A from the filamentous fungus Hypocrea jecorina. The structure reveals a general fold resembling that of the closest homolog with a high-resolution structure, Cel5A from Thermoascus aurantiacus. Consistent with previously described endoglucanase structures, the H. jecorina Cel5A active site contains a primarily hydrophobic substrate binding groove and a series of hydrogen bond networks surrounding two catalytic glutamates. The reported structure, however, demonstrates stark differences between side-chain identity, loop regions, and the number of disulfides. Such structural information may aid efforts to improve the stability of this protein for industrial use while maintaining enzymatic activity through revealing nonessential and immutable regions.

PubMed: 21898652
DOI: 10.1002/pro.730

Experimental method

X-RAY DIFFRACTION (2.05 Å)