1oi3
From Proteopedia
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| - | [[Image:1oi3. | + | [[Image:1oi3.jpg|left|200px]]<br /><applet load="1oi3" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1oi3" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1oi3, resolution 2.00Å" /> | caption="1oi3, resolution 2.00Å" /> | ||
'''X-RAY STRUCTURE OF THE DIHYDROXYACETONE KINASE FROM ESCHERICHIA COLI'''<br /> | '''X-RAY STRUCTURE OF THE DIHYDROXYACETONE KINASE FROM ESCHERICHIA COLI'''<br /> | ||
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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/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] | + | 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] Known structural/functional Site: <scene name='pdbsite=AC1:So4 Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OI3 OCA]. |
==Reference== | ==Reference== | ||
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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 Dec 18 17:44:50 2007'' |
Revision as of 15:35, 18 December 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 carbohydrate transporters and transcription regulators of, the phosphoenolpyruvate-dependent carbohydrate:phosphotransferase system., The core of the C-terminal domain has a fold similar to the C-terminal, domain of the cell-division protein FtsZ. A molecule of Dha is covalently, bound in hemiaminal linkage to the N epsilon 2 of His-230. The hemiaminal, does not participate in covalent catalysis but is the chemical basis for, discrimination between short-chain carbonyl compounds and polyols., Paralogs of Dha kinases occur in association with transcription regulators, of the TetR/QacR and the SorC families, pointing to their biological role, as sensors in signaling.
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 Known structural/functional Site: . 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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