1h5s
From Proteopedia
(New page: 200px<br /> <applet load="1h5s" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h5s, resolution 2.3Å" /> '''THYMIDYLYLTRANSFERAS...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1H5S is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/ ]] with TMP as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.24 2.7.7.24]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H5S OCA]]. | + | 1H5S is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/ ]] with TMP as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Glucose-1-phosphate_thymidylyltransferase Glucose-1-phosphate thymidylyltransferase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.24 2.7.7.24]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H5S OCA]]. |
==Reference== | ==Reference== | ||
Kinetic and crystallographic analyses support a sequential-ordered bi bi catalytic mechanism for Escherichia coli glucose-1-phosphate thymidylyltransferase., Zuccotti S, Zanardi D, Rosano C, Sturla L, Tonetti M, Bolognesi M, J Mol Biol. 2001 Nov 2;313(4):831-43. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11697907 11697907] | Kinetic and crystallographic analyses support a sequential-ordered bi bi catalytic mechanism for Escherichia coli glucose-1-phosphate thymidylyltransferase., Zuccotti S, Zanardi D, Rosano C, Sturla L, Tonetti M, Bolognesi M, J Mol Biol. 2001 Nov 2;313(4):831-43. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11697907 11697907] | ||
| + | [[Category: Glucose-1-phosphate thymidylyltransferase]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Bolognesi, M.]] | [[Category: Bolognesi, M.]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:35:09 2007'' |
Revision as of 09:30, 30 October 2007
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THYMIDYLYLTRANSFERASE COMPLEXED WITH TMP
Overview
Glucose-1-phosphate thymidylyltransferase is the first enzyme in the, biosynthesis of dTDP-l-rhamnose, the precursor of l-rhamnose, an essential, component of surface antigens, such as the O-lipopolysaccharide, mediating, virulence and adhesion to host tissues in many microorganisms. The enzyme, catalyses the formation of dTDP-glucose, from dTTP and glucose, 1-phosphate, as well as its pyrophosphorolysis. To shed more light on the, catalytic properties of glucose-1-phosphate thymidylyltransferase from, Escherichia coli, specifically distinguishing between ping pong and, sequential ordered bi bi reaction mechanisms, the enzyme kinetic, properties have been analysed in the presence of different substrates and, inhibitors. Moreover, three different complexes of glucose-1-phosphate, ... [(full description)]
About this Structure
1H5S is a [Protein complex] structure of sequences from [[1]] with TMP as [ligand]. Active as [Glucose-1-phosphate thymidylyltransferase], with EC number [2.7.7.24]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Kinetic and crystallographic analyses support a sequential-ordered bi bi catalytic mechanism for Escherichia coli glucose-1-phosphate thymidylyltransferase., Zuccotti S, Zanardi D, Rosano C, Sturla L, Tonetti M, Bolognesi M, J Mol Biol. 2001 Nov 2;313(4):831-43. PMID:11697907
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