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3pnq

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==Crystal Structure of E.coli Dha kinase DhaK (H56N) complex with Dha==
==Crystal Structure of E.coli Dha kinase DhaK (H56N) complex with Dha==
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<StructureSection load='3pnq' size='340' side='right' caption='[[3pnq]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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<StructureSection load='3pnq' size='340' side='right'caption='[[3pnq]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3pnq]] is a 4 chain structure with 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=3PNQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PNQ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3pnq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PNQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PNQ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2HA:DIHYDROXYACETONE'>2HA</scene></td></tr>
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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]] 2.2&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3pnk|3pnk]], [[3pnl|3pnl]], [[3pnm|3pnm]], [[3pno|3pno]]</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=2HA:DIHYDROXYACETONE'>2HA</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b1200, dhaK, JW5187, ycgT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>
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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=3pnq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pnq OCA], [https://pdbe.org/3pnq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pnq RCSB], [https://www.ebi.ac.uk/pdbsum/3pnq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pnq ProSAT]</span></td></tr>
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<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=3pnq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pnq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3pnq RCSB], [http://www.ebi.ac.uk/pdbsum/3pnq PDBsum]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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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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The Escherichia coli dihydroxyacetone (Dha) kinase is an unusual kinase because (i) it uses the phosphoenolpyruvate carbohydrate: phosphotransferase system (PTS) as the source of high-energy phosphate, (ii) the active site is formed by two subunits, and (iii) the substrate is covalently bound to His218(K)* of the DhaK subunit. The PTS transfers phosphate to DhaM, which in turn phosphorylates the permanently bound ADP coenzyme of DhaL. This phosphoryl group is subsequently transferred to the Dha substrate bound to DhaK. Here we report the crystal structure of the E. coli Dha kinase complex, DhaK-DhaL. The structure of the complex reveals that DhaK undergoes significant conformational changes to accommodate binding of DhaL. Combined mutagenesis and enzymatic activity studies of kinase mutants allow us to propose a catalytic mechanism for covalent Dha binding, phosphorylation, and release of the Dha-phosphate product. Our results show that His56(K) is involved in formation of the covalent hemiaminal bond with Dha. The structure of H56N(K) with noncovalently bound substrate reveals a somewhat different positioning of Dha in the binding pocket as compared to covalently bound Dha, showing that the covalent attachment to His218(K) orients the substrate optimally for phosphoryl transfer. Asp109(K) is critical for activity, likely acting as a general base activating the gamma-OH of Dha. Our results provide a comprehensive picture of the roles of the highly conserved active site residues of dihydroxyacetone kinases.
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Structural and mechanistic insight into covalent substrate binding by Escherichia coli dihydroxyacetone kinase.,Shi R, McDonald L, Cui Q, Matte A, Cygler M, Ekiel I Proc Natl Acad Sci U S A. 2011 Jan 5. PMID:21209328<ref>PMID:21209328</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Escherichia coli]]
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[[Category: Escherichia coli K-12]]
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[[Category: Structural genomic]]
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[[Category: Large Structures]]
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[[Category: Cygler, M]]
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[[Category: Cygler M]]
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[[Category: Ekiel, I]]
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[[Category: Ekiel I]]
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[[Category: Matte, A]]
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[[Category: Matte A]]
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[[Category: McDonald, L]]
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[[Category: McDonald L]]
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[[Category: Shi, R]]
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[[Category: Shi R]]
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[[Category: Bsgi]]
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[[Category: Transferase]]
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Current revision

Crystal Structure of E.coli Dha kinase DhaK (H56N) complex with Dha

PDB ID 3pnq

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