1oi3
From Proteopedia
(New page: 200px<br /> <applet load="1oi3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oi3, resolution 2.00Å" /> '''X-RAY STRUCTURE OF ...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1OI3 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 SO4 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=2.7.1.29 2.7.1.29]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OI3 OCA]]. | + | 1OI3 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 SO4 as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Glycerone_kinase Glycerone kinase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.29 2.7.1.29]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OI3 OCA]]. |
==Reference== | ==Reference== | ||
A mechanism of covalent substrate binding in the x-ray structure of subunit K of the Escherichia coli dihydroxyacetone kinase., Siebold C, Garcia-Alles LF, Erni B, Baumann U, Proc Natl Acad Sci U S A. 2003 Jul 8;100(14):8188-92. Epub 2003 Jun 17. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12813127 12813127] | A mechanism of covalent substrate binding in the x-ray structure of subunit K of the Escherichia coli dihydroxyacetone kinase., Siebold C, Garcia-Alles LF, Erni B, Baumann U, Proc Natl Acad Sci U S A. 2003 Jul 8;100(14):8188-92. Epub 2003 Jun 17. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12813127 12813127] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| + | [[Category: Glycerone kinase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Baumann, U.]] | [[Category: Baumann, U.]] | ||
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[[Category: ycgt]] | [[Category: ycgt]] | ||
| - | ''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 12:19:09 2007'' |
Revision as of 10:14, 30 October 2007
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X-RAY STRUCTURE OF THE DIHYDROXYACETONE KINASE FROM ESCHERICHIA COLI
Overview
Dihydroxyacetone (Dha) kinases are homologous proteins that use different, phosphoryl donors, a multiphosphoryl protein of the, phosphoenolpyruvate-dependent carbohydrate:phosphotransferase system in, bacteria, ATP in animals, plants, and some bacteria. The Dha kinase of, Escherichia coli consists of three subunits, DhaK and DhaL, which are, colinear to the ATP-dependent Dha kinases of eukaryotes, and the, multiphosphoryl protein DhaM. Here we show the crystal structure of the, DhaK subunit in complex with Dha at 1.75 A resolution. DhaK is a homodimer, with a fold consisting of two six-stranded mixed beta-sheets surrounded by, nine alpha-helices and a beta-ribbon covering the exposed edge strand of, one sheet. The core of the N-terminal domain has an alpha/beta fold common, to subunits of ... [(full description)]
About this Structure
1OI3 is a [Single protein] structure of sequence from [Escherichia coli] with SO4 as [ligand]. Active as [Glycerone kinase], with EC number [2.7.1.29]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
A mechanism of covalent substrate binding in the x-ray structure of subunit K of the Escherichia coli dihydroxyacetone kinase., Siebold C, Garcia-Alles LF, Erni B, Baumann U, Proc Natl Acad Sci U S A. 2003 Jul 8;100(14):8188-92. Epub 2003 Jun 17. PMID:12813127
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