1tjs: Difference between revisions
New page: left|200px<br /> <applet load="1tjs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tjs, resolution 2.20Å" /> '''E. COLI THYMIDYLATE... |
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==About this Structure== | ==About this Structure== | ||
1TJS 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 PO4 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=2.1.1.45 2.1.1.45]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TJS OCA]]. | 1TJS 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 PO4 as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Transferase Transferase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.45 2.1.1.45]]. Structure known Active Site: ACT. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TJS OCA]]. | ||
==Reference== | ==Reference== | ||
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[[Category: transferase (methyltransferase)]] | [[Category: transferase (methyltransferase)]] | ||
''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 08:29:54 2007'' | ||
Revision as of 09:25, 30 October 2007
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E. COLI THYMIDYLATE SYNTHASE
OverviewOverview
BACKGROUND: Enzymes have evolved to recognise their target substrates with, exquisite selectivity and specificity. Whether fragments of the, substrate--perhaps never available to the evolving enzyme--are bound in, the same manner as the parent substrate addresses the fundamental basis of, specificity. An understanding of the relative contributions of individual, portions of ligand molecules to the enzyme-binding interaction may offer, considerable insight into the principles of substrate recognition., RESULTS: We report 12 crystal structures of Escherichia coli thymidylate, synthase in complexes with available fragments of the substrate (dUMP), both with and without the presence of a cofactor analogue. The structures, display considerable fidelity of binding mode and interactions. These, ... [(full description)]
About this StructureAbout this Structure
1TJS is a [Single protein] structure of sequence from [Escherichia coli] with PO4 as [ligand]. Active as [Transferase], with EC number [2.1.1.45]. Structure known Active Site: ACT. Full crystallographic information is available from [OCA].
ReferenceReference
The additivity of substrate fragments in enzyme-ligand binding., Stout TJ, Sage CR, Stroud RM, Structure. 1998 Jul 15;6(7):839-48. PMID:9687366
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