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1oi2

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[[Image:1oi2.gif|left|200px]]<br />
 
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<applet load="1oi2" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1oi2, resolution 1.75&Aring;" />
 
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'''X-RAY STRUCTURE OF THE DIHYDROXYACETONE KINASE FROM ESCHERICHIA COLI'''<br />
 
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==Overview==
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==X-ray structure of the dihydroxyacetone kinase from Escherichia coli==
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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 ... [[http://ispc.weizmann.ac.il/pmbin/getpm?12813127 (full description)]]
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<StructureSection load='1oi2' size='340' side='right'caption='[[1oi2]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<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>
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1OI2 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 and GOL as [[http://en.wikipedia.org/wiki/ligands ligands]]. 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]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OI2 OCA]].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
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<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>
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==Reference==
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<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>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=12813127 12813127]
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oi/1oi2_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1oi2 ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Glycerone kinase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Baumann U]]
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[[Category: Baumann, U.]]
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[[Category: Erni B]]
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[[Category: Erni, B.]]
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[[Category: Garcia-Alles L-F]]
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[[Category: Garcia-Alles, L.F.]]
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[[Category: Siebold C]]
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[[Category: Siebold, C.]]
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[[Category: GOL]]
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[[Category: SO4]]
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[[Category: dihydroxyacetone kinase]]
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[[Category: kinase]]
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[[Category: ycgt]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:18:50 2007''
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Current revision

X-ray structure of the dihydroxyacetone kinase from Escherichia coli

PDB ID 1oi2

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