1C8U

CRYSTAL STRUCTURE OF THE E.COLI THIOESTERASE II, A HOMOLOGUE OF THE HUMAN NEF-BINDING ENZYME

Summary for 1C8U

• Entry DOI: 10.2210/pdb1c8u/pdb
• Descriptor: ACYL-COA THIOESTERASE II, LAURYL DIMETHYLAMINE-N-OXIDE (3 entities in total)
• Functional Keywords: internal repeats, hydrolase
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 64204.93

Authors

Li, J.,Derewenda, Z.S. (deposition date: 1999-07-29, release date: 2000-07-14, Last modification date: 2024-02-07)

Primary citation

Li, J.,Derewenda, U.,Dauter, Z.,Smith, S.,Derewenda, Z.S.
Crystal structure of the Escherichia coli thioesterase II, a homolog of the human Nef binding enzyme.
Nat.Struct.Biol., 7:555-559, 2000

PubMed Abstract: Here we report the solution and refinement at 1.9 A resolution of the crystal structure of the Escherichia coli medium chain length acyl-CoA thioesterase II. This enzyme is a close homolog of the human protein that interacts with the product of the HIV-1 Nef gene, sharing 45% amino acid sequence identity with it. The structure of the E. coli thioesterase II reveals a new tertiary fold, a 'double hot dog', showing an internal repeat with a basic unit that is structurally similar to the recently described beta-hydroxydecanoyl thiol ester dehydrase. The catalytic site, inferred from the crystal structure and verified by site directed mutagenesis, involves novel chemistry and includes Asp 204, Gln 278 and Thr 228, which synergistically activate a nucleophilic water molecule.

PubMed: 10876240
DOI: 10.1038/76776

Experimental method

X-RAY DIFFRACTION (1.9 Å)