1oi2
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1oi2.jpg|left|200px]] | [[Image:1oi2.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1oi2", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | | | + | --> |
| - | | | + | {{STRUCTURE_1oi2| PDB=1oi2 | SCENE= }} |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''X-RAY STRUCTURE OF THE DIHYDROXYACETONE KINASE FROM ESCHERICHIA COLI''' | '''X-RAY STRUCTURE OF THE DIHYDROXYACETONE KINASE FROM ESCHERICHIA COLI''' | ||
| Line 30: | Line 27: | ||
[[Category: Garcia-Alles, L F.]] | [[Category: Garcia-Alles, L F.]] | ||
[[Category: Siebold, C.]] | [[Category: Siebold, C.]] | ||
| - | [[Category: | + | [[Category: Dihydroxyacetone kinase]] |
| - | [[Category: | + | [[Category: Kinase]] |
| - | [[Category: | + | [[Category: Ycgt]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:52:25 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 00:52, 3 May 2008
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
1OI2 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 Page seeded by OCA on Sat May 3 03:52:25 2008
