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| | ==X-ray structure of the dihydroxyacetone kinase from Escherichia coli== | | ==X-ray structure of the dihydroxyacetone kinase from Escherichia coli== |
| - | <StructureSection load='1oi2' size='340' side='right' caption='[[1oi2]], [[Resolution|resolution]] 1.75Å' scene=''> | + | <StructureSection load='1oi2' size='340' side='right'caption='[[1oi2]], [[Resolution|resolution]] 1.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1oi2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OI2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OI2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1oi2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OI2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OI2 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1oi3|1oi3]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1oi2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oi2 OCA], [https://pdbe.org/1oi2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oi2 RCSB], [https://www.ebi.ac.uk/pdbsum/1oi2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oi2 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oi2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oi2 OCA], [http://pdbe.org/1oi2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1oi2 RCSB], [http://www.ebi.ac.uk/pdbsum/1oi2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1oi2 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DHAK_ECOLI DHAK_ECOLI]] Dihydroxyacetone binding subunit of the dihydroxyacetone kinase, which is responsible for phosphorylating dihydroxyacetone. Binds covalently dihydroxyacetone in hemiaminal linkage. Acts also as a corepressor of DhaR by binding to its sensor domain, in the absence of dihydroxyacetone. | + | [https://www.uniprot.org/uniprot/DHAK_ECOLI DHAK_ECOLI] Dihydroxyacetone binding subunit of the dihydroxyacetone kinase, which is responsible for phosphorylating dihydroxyacetone. Binds covalently dihydroxyacetone in hemiaminal linkage. Acts also as a corepressor of DhaR by binding to its sensor domain, in the absence of dihydroxyacetone. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oi/1oi2_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oi/1oi2_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| - | [[Category: Glycerone kinase]] | + | [[Category: Large Structures]] |
| - | [[Category: Baumann, U]] | + | [[Category: Baumann U]] |
| - | [[Category: Erni, B]] | + | [[Category: Erni B]] |
| - | [[Category: Garcia-Alles, L F]] | + | [[Category: Garcia-Alles L-F]] |
| - | [[Category: Siebold, C]] | + | [[Category: Siebold C]] |
| - | [[Category: Dihydroxyacetone kinase]]
| + | |
| - | [[Category: Kinase]]
| + | |
| - | [[Category: Ycgt]]
| + | |
| Structural highlights
Function
DHAK_ECOLI Dihydroxyacetone binding subunit of the dihydroxyacetone kinase, which is responsible for phosphorylating dihydroxyacetone. Binds covalently dihydroxyacetone in hemiaminal linkage. Acts also as a corepressor of DhaR by binding to its sensor domain, in the absence of dihydroxyacetone.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Siebold C, Garcia-Alles LF, Erni B, Baumann U. A mechanism of covalent substrate binding in the x-ray structure of subunit K of the Escherichia coli dihydroxyacetone kinase. Proc Natl Acad Sci U S A. 2003 Jul 8;100(14):8188-92. Epub 2003 Jun 17. PMID:12813127 doi:http://dx.doi.org/10.1073/pnas.0932787100
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