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 1.9&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1c8u.gif|left|200px]]<br /><applet load="1c8u" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1c8u.gif|left|200px]]<br /><applet load="1c8u" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1c8u, resolution 1.9&Aring;" />
caption="1c8u, resolution 1.9&Aring;" />
'''CRYSTAL STRUCTURE OF THE E.COLI THIOESTERASE II, A HOMOLOGUE OF THE HUMAN NEF-BINDING ENZYME'''<br />
'''CRYSTAL STRUCTURE OF THE E.COLI THIOESTERASE II, A HOMOLOGUE OF THE HUMAN NEF-BINDING ENZYME'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1C8U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with LDA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1C8U OCA].
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1C8U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=LDA:'>LDA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C8U OCA].
==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Derewenda, Z.S.]]
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[[Category: Derewenda, Z S.]]
[[Category: Li, J.]]
[[Category: Li, J.]]
[[Category: LDA]]
[[Category: LDA]]
[[Category: internal repeats]]
[[Category: internal repeats]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:15:56 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:03:37 2008''

Revision as of 10:03, 21 February 2008


1c8u, resolution 1.9Å

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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 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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