3RBT

Crystal structure of glutathione S-transferase Omega 3 from the silkworm Bombyx mori

Summary for 3RBT

• Entry DOI: 10.2210/pdb3rbt/pdb
• Descriptor: Glutathione transferase o1, GLYCEROL (3 entities in total)
• Functional Keywords: glutathione s-transferase omega3, transferase
• Biological source: Bombyx mori (silk moth, silkworm)
• Total number of polymer chains: 4
• Total formula weight: 117986.62

Authors

Chen, B.-Y.,Ma, X.-X.,Tan, X.,Yang, J.-P.,Zhang, N.-N.,Li, W.-F.,Chen, Y.,Xia, Q.,Zhou, C.-Z. (deposition date: 2011-03-29, release date: 2011-08-10, Last modification date: 2023-11-01)

Primary citation

Chen, B.-Y.,Ma, X.-X.,Guo, P.-C.,Tan, X.,Li, W.-F.,Yang, J.-P.,Zhang, N.-N.,Chen, Y.,Xia, Q.,Zhou, C.-Z.
Structure-guided activity restoration of the silkworm glutathione transferase Omega GSTO3-3
J.Mol.Biol., 412:204-211, 2011

PubMed Abstract: Glutathione transferases (GSTs) are ubiquitous detoxification enzymes that conjugate hydrophobic xenobiotics with reduced glutathione. The silkworm Bombyx mori encodes four isoforms of GST Omega (GSTO), featured with a catalytic cysteine, except that bmGSTO3-3 has an asparagine substitution of this catalytic residue. Here, we determined the 2.20-Å crystal structure of bmGSTO3-3, which shares a typical GST overall structure. However, the extended C-terminal segment that exists in all the four bmGSTOs occupies the G-site of bmGSTO3-3 and makes it unworkable, as shown by the activity assays. Upon mutation of Asn29 to Cys and truncation of the C-terminal segment, the in vitro GST activity of bmGSTO3-3 could be restored. These findings provided structural insights into the activity regulation of GSTOs.

PubMed: 21816159
DOI: 10.1016/j.jmb.2011.07.019

Experimental method

X-RAY DIFFRACTION (2.2 Å)