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| - | [[Image:1oi2.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1oi2| PDB=1oi2 | SCENE= }} | | {{STRUCTURE_1oi2| PDB=1oi2 | SCENE= }} |
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| - | '''X-RAY STRUCTURE OF THE DIHYDROXYACETONE KINASE FROM ESCHERICHIA COLI'''
| + | ===X-RAY STRUCTURE OF THE DIHYDROXYACETONE KINASE FROM ESCHERICHIA COLI=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12813127}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12813127 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_12813127}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Kinase]] | | [[Category: Kinase]] |
| | [[Category: Ycgt]] | | [[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 Tue Jul 29 09:22:10 2008'' |
Revision as of 06:22, 29 July 2008
Template:STRUCTURE 1oi2
X-RAY STRUCTURE OF THE DIHYDROXYACETONE KINASE FROM ESCHERICHIA COLI
Template:ABSTRACT PUBMED 12813127
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 Tue Jul 29 09:22:10 2008
