2PMT

GLUTATHIONE TRANSFERASE FROM PROTEUS MIRABILIS

Summary for 2PMT

• Entry DOI: 10.2210/pdb2pmt/pdb
• Descriptor: GLUTATHIONE TRANSFERASE, GLUTATHIONE (2 entities in total)
• Functional Keywords: transferase, glutathione-conjugating, a putative oxidoreductase
• Biological source: Proteus mirabilis
• Cellular location: Cytoplasm: P15214
• Total number of polymer chains: 4
• Total formula weight: 92754.27

Authors

Rossjohn, J.,Polekhina, G.,Feil, S.C.,Allocati, N.,Masulli, M.,Diilio, C.,Parker, M.W. (deposition date: 1998-04-28, release date: 1999-04-27, Last modification date: 2024-06-05)

Primary citation

Rossjohn, J.,Polekhina, G.,Feil, S.C.,Allocati, N.,Masulli, M.,De Illio, C.,Parker, M.W.
A mixed disulfide bond in bacterial glutathione transferase: functional and evolutionary implications.
Structure, 6:721-734, 1998

PubMed Abstract: Glutathione S-transferases (GSTs) are a multifunctional group of enzymes, widely distributed in aerobic organisms, that have a critical role in the cellular detoxification process. Unlike their mammalian counterparts, bacterial GSTs often catalyze quite specific reactions, suggesting that their roles in bacteria might be different. The GST from Proteus mirabilis (PmGST B1-1) is known to bind certain antibiotics tightly and reduce the antimicrobial activity of beta-lactam drugs. Hence, bacterial GSTs may play a part in bacterial resistance towards antibiotics and are the subject of intense interest.

PubMed: 9655824
DOI: 10.1016/S0969-2126(98)00074-4

Experimental method

X-RAY DIFFRACTION (2.7 Å)