1c8u
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(New page: 200px<br /><applet load="1c8u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c8u, resolution 1.9Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 10:08, 20 November 2007
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CRYSTAL STRUCTURE OF THE E.COLI THIOESTERASE II, A HOMOLOGUE OF THE HUMAN NEF-BINDING ENZYME
Overview
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.
About this Structure
1C8U is a Single protein structure of sequence from Escherichia coli with LDA as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of the Escherichia coli thioesterase II, a homolog of the human Nef binding enzyme., Li J, Derewenda U, Dauter Z, Smith S, Derewenda ZS, Nat Struct Biol. 2000 Jul;7(7):555-9. PMID:10876240
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