1w77
From Proteopedia
(New page: 200px<br /> <applet load="1w77" size="450" color="white" frame="true" align="right" spinBox="true" caption="1w77, resolution 2.00Å" /> '''2C-METHYL-D-ERYTHRI...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1W77 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]] with CD, CU and C5P as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.60 2.7.7.60]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1W77 OCA]]. | + | 1W77 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]] with CD, CU and C5P as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/2-C-methyl-D-erythritol_4-phosphate_cytidylyltransferase 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.60 2.7.7.60]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1W77 OCA]]. |
==Reference== | ==Reference== | ||
The crystal structure of a plant 2C-methyl-D-erythritol 4-phosphate cytidylyltransferase exhibits a distinct quaternary structure compared to bacterial homologues and a possible role in feedback regulation for cytidine monophosphate., Gabrielsen M, Kaiser J, Rohdich F, Eisenreich W, Laupitz R, Bacher A, Bond CS, Hunter WN, FEBS J. 2006 Mar;273(5):1065-73. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16478479 16478479] | The crystal structure of a plant 2C-methyl-D-erythritol 4-phosphate cytidylyltransferase exhibits a distinct quaternary structure compared to bacterial homologues and a possible role in feedback regulation for cytidine monophosphate., Gabrielsen M, Kaiser J, Rohdich F, Eisenreich W, Laupitz R, Bacher A, Bond CS, Hunter WN, FEBS J. 2006 Mar;273(5):1065-73. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16478479 16478479] | ||
| + | [[Category: 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase]] | ||
[[Category: Arabidopsis thaliana]] | [[Category: Arabidopsis thaliana]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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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 14:20:02 2007'' |
Revision as of 12:15, 30 October 2007
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2C-METHYL-D-ERYTHRITOL 4-PHOSPHATE CYTIDYLYLTRANSFERASE (ISPD) FROM ARABIDOPSIS THALIANA
Overview
The homodimeric 2C-methyl-D-erythritol 4-phosphate cytidylyltransferase, contributes to the nonmevalonate pathway of isoprenoid biosynthesis. The, crystal structure of the catalytic domain of the recombinant enzyme, derived from the plant Arabidopsis thaliana has been solved by molecular, replacement and refined to 2.0 A resolution. The structure contains, cytidine monophosphate bound in the active site, a ligand that has been, acquired from the bacterial expression system, and this observation, suggests a mechanism for feedback regulation of enzyme activity., Comparisons with bacterial enzyme structures, in particular the enzyme, from Escherichia coli, indicate that whilst individual subunits overlay, well, the arrangement of subunits in each functional dimer is different., That distinct ... [(full description)]
About this Structure
1W77 is a [Single protein] structure of sequence from [Arabidopsis thaliana] with CD, CU and C5P as [ligands]. Active as [2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase], with EC number [2.7.7.60]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
The crystal structure of a plant 2C-methyl-D-erythritol 4-phosphate cytidylyltransferase exhibits a distinct quaternary structure compared to bacterial homologues and a possible role in feedback regulation for cytidine monophosphate., Gabrielsen M, Kaiser J, Rohdich F, Eisenreich W, Laupitz R, Bacher A, Bond CS, Hunter WN, FEBS J. 2006 Mar;273(5):1065-73. PMID:16478479
Page seeded by OCA on Tue Oct 30 14:20:02 2007
Categories: 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase | Arabidopsis thaliana | Single protein | Bacher, A. | Bond, C.S. | Eisenreich, W. | Gabrielsen, M. | Hunter, W.N. | Kaiser, J. | Rohdich, F. | C5P | CD | CU | Cytidylyltransferase | Isoprenoid | Non-mevalonate pathway | Plantherbicide | Transferase
