1oi3
From Proteopedia
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| - | [[Image:1oi3.jpg|left|200px]] | + | [[Image:1oi3.jpg|left|200px]] |
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| - | '''X-RAY STRUCTURE OF THE DIHYDROXYACETONE KINASE FROM ESCHERICHIA COLI''' | + | {{Structure |
| + | |PDB= 1oi3 |SIZE=350|CAPTION= <scene name='initialview01'>1oi3</scene>, resolution 2.00Å | ||
| + | |SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+B'>AC1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''X-RAY STRUCTURE OF THE DIHYDROXYACETONE KINASE FROM ESCHERICHIA COLI''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1OI3 is a [ | + | 1OI3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.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:// | + | 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://www.ncbi.nlm.nih.gov/pubmed/12813127 12813127] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Glycerone kinase]] | [[Category: Glycerone kinase]] | ||
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[[Category: ycgt]] | [[Category: ycgt]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:11:13 2008'' |
Revision as of 11:11, 20 March 2008
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| , resolution 2.00Å | |||||||
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| Sites: | |||||||
| Ligands: | |||||||
| Activity: | Glycerone kinase, with EC number 2.7.1.29 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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