2j4q
From Proteopedia
(New page: 200px<br /> <applet load="2j4q" size="450" color="white" frame="true" align="right" spinBox="true" caption="2j4q, resolution 2.60Å" /> '''CRYSTAL STRUCTURE O...) |
|||
| Line 8: | Line 8: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2J4Q 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 MG, TYD and TTP 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=3.5.4.13 3.5.4.13]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2J4Q OCA]]. | + | 2J4Q 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 MG, TYD and TTP as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/dCTP_deaminase dCTP deaminase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.13 3.5.4.13]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2J4Q OCA]]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| + | [[Category: dCTP deaminase]] | ||
[[Category: Bynck, J.H.]] | [[Category: Bynck, J.H.]] | ||
[[Category: Fanoe, M.]] | [[Category: Fanoe, M.]] | ||
| Line 28: | Line 29: | ||
[[Category: trimer]] | [[Category: trimer]] | ||
| - | ''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 13:45:34 2007'' |
Revision as of 11:40, 30 October 2007
|
CRYSTAL STRUCTURE OF A E138A ESCHERICHIA COLI DCTP DEAMINASE MUTANT ENZYME IN COMPLEX WITH DTTP
Overview
The trimeric dCTP deaminase produces dUTP that is hydrolysed to dUMP by, the structurally closely related dUTPase. This pathway provides 70-80% of, the total dUMP as a precursor for dTTP. Accordingly, dCTP deaminase is, regulated by dTTP, which increases the substrate concentration for, half-maximal activity and the cooperativity of dCTP saturation. Likewise, increasing concentrations of dCTP increase the cooperativity of dTTP, inhibition. Previous structural studies showed that the complexes of, inactive mutant protein, E138A, with dUTP or dCTP bound, and wild-type, enzyme with dUTP bound were all highly similar and characterized by having, an ordered C-terminal. When comparing with a new structure in which dTTP, is bound to the active site of E138A, the region between Val120 and His125, ... [(full description)]
About this Structure
2J4Q is a [Single protein] structure of sequence from [Escherichia coli] with MG, TYD and TTP as [ligands]. Active as [dCTP deaminase], with EC number [3.5.4.13]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Regulation of dCTP deaminase from Escherichia coli by nonallosteric dTTP binding to an inactive form of the enzyme., Johansson E, Thymark M, Bynck JH, Fano M, Larsen S, Willemoes M, FEBS J. 2007 Aug;274(16):4188-98. Epub 2007 Jul 25. PMID:17651436
Page seeded by OCA on Tue Oct 30 13:45:34 2007
Categories: Escherichia coli | Single protein | DCTP deaminase | Bynck, J.H. | Fanoe, M. | Johansson, E. | Larsen, S. | Thymark, M. | Willemoes, M. | MG | TTP | TYD | Dctp deaminase | Hydrolase | Nucleotide metabolism | Trimer
