1k9v

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(New page: 200px<br /><applet load="1k9v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k9v, resolution 2.4&Aring;" /> '''Structural evidence f...)
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[[Image:1k9v.jpg|left|200px]]<br /><applet load="1k9v" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1k9v.jpg|left|200px]]<br /><applet load="1k9v" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1k9v, resolution 2.4&Aring;" />
caption="1k9v, resolution 2.4&Aring;" />
'''Structural evidence for ammonia tunelling across the (beta-alpha)8-barrel of the imidazole glycerol phosphate synthase bienzyme complex'''<br />
'''Structural evidence for ammonia tunelling across the (beta-alpha)8-barrel of the imidazole glycerol phosphate synthase bienzyme complex'''<br />
==Overview==
==Overview==
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Since reactive ammonia is not available under physiological conditions, glutamine is used as a source for the incorporation of nitrogen in a, number of metabolic pathway intermediates. The heterodimeric ImGP synthase, that links histidine and purine biosynthesis belongs to the family of, glutamine amidotransferases in which the glutaminase activity is coupled, with a subsequent synthase activity specific for each member of the enzyme, family. Its X-ray structure from the hyperthermophile Thermotoga maritima, shows that the glutaminase subunit is associated with the N-terminal face, of the (beta alpha)(8) barrel cyclase subunit. The complex reveals a, putative tunnel for the transfer of ammonia over a distance of 25 A., Although ammonia tunneling has been reported for glutamine, amidotransferases, the ImGP synthase has evolved a novel mechanism, which, extends the known functional properties of the versatile (beta alpha)(8), barrel fold.
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Since reactive ammonia is not available under physiological conditions, glutamine is used as a source for the incorporation of nitrogen in a number of metabolic pathway intermediates. The heterodimeric ImGP synthase that links histidine and purine biosynthesis belongs to the family of glutamine amidotransferases in which the glutaminase activity is coupled with a subsequent synthase activity specific for each member of the enzyme family. Its X-ray structure from the hyperthermophile Thermotoga maritima shows that the glutaminase subunit is associated with the N-terminal face of the (beta alpha)(8) barrel cyclase subunit. The complex reveals a putative tunnel for the transfer of ammonia over a distance of 25 A. Although ammonia tunneling has been reported for glutamine amidotransferases, the ImGP synthase has evolved a novel mechanism, which extends the known functional properties of the versatile (beta alpha)(8) barrel fold.
==About this Structure==
==About this Structure==
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1K9V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with ACY as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1K9V OCA].
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1K9V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with <scene name='pdbligand=ACY:'>ACY</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K9V OCA].
==Reference==
==Reference==
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[[Category: Douangamath, A.]]
[[Category: Douangamath, A.]]
[[Category: Sterner, R.]]
[[Category: Sterner, R.]]
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[[Category: Vega-Fernandez, M.C.]]
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[[Category: Vega-Fernandez, M C.]]
[[Category: Walker, M.]]
[[Category: Walker, M.]]
[[Category: Wilmanns, M.]]
[[Category: Wilmanns, M.]]
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[[Category: x-ray structure]]
[[Category: x-ray structure]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:59:13 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:31:42 2008''

Revision as of 11:31, 21 February 2008


1k9v, resolution 2.4Å

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Structural evidence for ammonia tunelling across the (beta-alpha)8-barrel of the imidazole glycerol phosphate synthase bienzyme complex

Overview

Since reactive ammonia is not available under physiological conditions, glutamine is used as a source for the incorporation of nitrogen in a number of metabolic pathway intermediates. The heterodimeric ImGP synthase that links histidine and purine biosynthesis belongs to the family of glutamine amidotransferases in which the glutaminase activity is coupled with a subsequent synthase activity specific for each member of the enzyme family. Its X-ray structure from the hyperthermophile Thermotoga maritima shows that the glutaminase subunit is associated with the N-terminal face of the (beta alpha)(8) barrel cyclase subunit. The complex reveals a putative tunnel for the transfer of ammonia over a distance of 25 A. Although ammonia tunneling has been reported for glutamine amidotransferases, the ImGP synthase has evolved a novel mechanism, which extends the known functional properties of the versatile (beta alpha)(8) barrel fold.

About this Structure

1K9V is a Single protein structure of sequence from Thermotoga maritima with as ligand. Full crystallographic information is available from OCA.

Reference

Structural evidence for ammonia tunneling across the (beta alpha)(8) barrel of the imidazole glycerol phosphate synthase bienzyme complex., Douangamath A, Walker M, Beismann-Driemeyer S, Vega-Fernandez MC, Sterner R, Wilmanns M, Structure. 2002 Feb;10(2):185-93. PMID:11839304

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