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3pnl

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Revision as of 14:43, 25 December 2014

Crystal Structure of E.coli Dha kinase DhaK-DhaL complex

Structural highlights

3pnl is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	3pnq, 3pnk, 3pnm, 3pno
Gene:	b1200, dhaK, JW5187, ycgT (Escherichia coli), b1199, dhaL, JW5186, ycgS (Escherichia coli)
Resources:	FirstGlance, OCA, RCSB, PDBsum

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. [DHAL_ECOLI] ADP-binding subunit of the dihydroxyacetone kinase, which is responsible for phosphorylating dihydroxyacetone. DhaL-ADP receives a phosphoryl group from DhaM and transmits it to dihydroxyacetone. DhaL-ADP acts also as a coactivator by binding to the sensor domain of DhaR. DhaL-ATP is inactive.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Shi R, McDonald L, Cui Q, Matte A, Cygler M, Ekiel I. Structural and mechanistic insight into covalent substrate binding by Escherichia coli dihydroxyacetone kinase. Proc Natl Acad Sci U S A. 2011 Jan 5. PMID:21209328 doi:10.1073/pnas.1012596108

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3pnl"

@@ Line 8: / Line 8: @@
 <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=3pnl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pnl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3pnl RCSB], [http://www.ebi.ac.uk/pdbsum/3pnl PDBsum]</span></td></tr>
 </table>
+== 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. [[http://www.uniprot.org/uniprot/DHAL_ECOLI DHAL_ECOLI]] ADP-binding subunit of the dihydroxyacetone kinase, which is responsible for phosphorylating dihydroxyacetone. DhaL-ADP receives a phosphoryl group from DhaM and transmits it to dihydroxyacetone. DhaL-ADP acts also as a coactivator by binding to the sensor domain of DhaR. DhaL-ATP is inactive.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

3pnl

From Proteopedia

Revision as of 14:43, 25 December 2014

Crystal Structure of E.coli Dha kinase DhaK-DhaL complex

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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