2f0x

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(New page: 200px<br /> <applet load="2f0x" size="450" color="white" frame="true" align="right" spinBox="true" caption="2f0x, resolution 2.300&Aring;" /> '''Crystal structure ...)
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<applet load="2f0x" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="2f0x, resolution 2.300&Aring;" />
'''Crystal structure and function of human thioesterase superfamily member 2(THEM2)'''<br />
'''Crystal structure and function of human thioesterase superfamily member 2(THEM2)'''<br />
==Overview==
==Overview==
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Hotdog-fold has been identified in more than 1000 proteins, yet many of, which in eukaryotes are less studied. No structural or functional studies, of human thioesterase superfamily member 2 (hTHEM2) have been reported, before. Since hTHEM2 exhibits about 20% sequence identity to Escherichia, coli PaaI protein, it was proposed to be a thioesterase with a, hotdog-fold. Here, we report the crystallographic structure of recombinant, hTHEM2, determined by the single-wavelength anomalous dispersion method at, 2.3A resolution. This structure demonstrates that hTHEM2 indeed contains a, hotdog-fold and forms a back-to-back tetramer as other hotdog proteins., Based on structural and sequence conservation, the thioesterase active, site in hTHEM2 is predicted. The structure and substrate specificity are, most similar to those of the bacterial phenylacetyl-CoA hydrolase. Asp65, located on the central alpha-helix of subunit B, was shown by, site-directed mutagenesis to be essential to catalysis.
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Hotdog-fold has been identified in more than 1000 proteins, yet many of which in eukaryotes are less studied. No structural or functional studies of human thioesterase superfamily member 2 (hTHEM2) have been reported before. Since hTHEM2 exhibits about 20% sequence identity to Escherichia coli PaaI protein, it was proposed to be a thioesterase with a hotdog-fold. Here, we report the crystallographic structure of recombinant hTHEM2, determined by the single-wavelength anomalous dispersion method at 2.3A resolution. This structure demonstrates that hTHEM2 indeed contains a hotdog-fold and forms a back-to-back tetramer as other hotdog proteins. Based on structural and sequence conservation, the thioesterase active site in hTHEM2 is predicted. The structure and substrate specificity are most similar to those of the bacterial phenylacetyl-CoA hydrolase. Asp65, located on the central alpha-helix of subunit B, was shown by site-directed mutagenesis to be essential to catalysis.
==About this Structure==
==About this Structure==
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2F0X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2F0X OCA].
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2F0X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F0X OCA].
==Reference==
==Reference==
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[[Category: hot dog fold]]
[[Category: hot dog fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 21:57:57 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:16:33 2008''

Revision as of 15:16, 21 February 2008

Image:2f0x.gif

2f0x, resolution 2.300Å

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Crystal structure and function of human thioesterase superfamily member 2(THEM2)

Overview

Hotdog-fold has been identified in more than 1000 proteins, yet many of which in eukaryotes are less studied. No structural or functional studies of human thioesterase superfamily member 2 (hTHEM2) have been reported before. Since hTHEM2 exhibits about 20% sequence identity to Escherichia coli PaaI protein, it was proposed to be a thioesterase with a hotdog-fold. Here, we report the crystallographic structure of recombinant hTHEM2, determined by the single-wavelength anomalous dispersion method at 2.3A resolution. This structure demonstrates that hTHEM2 indeed contains a hotdog-fold and forms a back-to-back tetramer as other hotdog proteins. Based on structural and sequence conservation, the thioesterase active site in hTHEM2 is predicted. The structure and substrate specificity are most similar to those of the bacterial phenylacetyl-CoA hydrolase. Asp65, located on the central alpha-helix of subunit B, was shown by site-directed mutagenesis to be essential to catalysis.

About this Structure

2F0X is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of human thioesterase superfamily member 2., Cheng Z, Song F, Shan X, Wei Z, Wang Y, Dunaway-Mariano D, Gong W, Biochem Biophys Res Commun. 2006 Oct 13;349(1):172-7. Epub 2006 Aug 14. PMID:16934754

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