3ct4
From Proteopedia
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- | {{STRUCTURE_3ct4| PDB=3ct4 | SCENE= }} | ||
- | ===Structure of Dha-kinase subunit DhaK from L. Lactis=== | ||
- | {{ABSTRACT_PUBMED_18957416}} | ||
- | == | + | ==Structure of Dha-kinase subunit DhaK from L. Lactis== |
- | [[http://www.uniprot.org/uniprot/DHAK_LACLA DHAK_LACLA | + | <StructureSection load='3ct4' size='340' side='right'caption='[[3ct4]], [[Resolution|resolution]] 2.50Å' scene=''> |
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[3ct4]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactococcus_lactis_subsp._lactis Lactococcus lactis subsp. lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CT4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CT4 FirstGlance]. <br> | ||
+ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.498Å</td></tr> | ||
+ | <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> | ||
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ct4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ct4 OCA], [https://pdbe.org/3ct4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ct4 RCSB], [https://www.ebi.ac.uk/pdbsum/3ct4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ct4 ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/DHAK_LACLA DHAK_LACLA] Dihydroxyacetone binding subunit of the dihydroxyacetone kinase, which is responsible for phosphorylating dihydroxyacetone. | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ct/3ct4_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </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=3ct4 ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Bacterial dihydroxyacetone (Dha) kinases do not exchange the ADP for ATP but utilize a subunit of the phosphoenolpyruvate carbohydrate phosphotransferase system for in situ rephosphorylation of a permanently bound ADP-cofactor. Here we report the 2.1-angstroms crystal structure of the transient complex between the phosphotransferase subunit DhaM of the phosphotransferase system and the nucleotide binding subunit DhaL of the Dha kinase of Lactococcus lactis, the 1.1-angstroms structure of the free DhaM dimer, and the 2.5-angstroms structure of the Dha-binding DhaK subunit. Conserved salt bridges and an edge-to-plane stacking contact between two tyrosines serve to orient DhaL relative to the DhaM dimer. The distance between the imidazole Nepsilon2 of the DhaM His-10 and the beta-phosphate oxygen of ADP, between which the gamma-phosphate is transferred, is 4.9 angstroms. An invariant arginine, which is essential for activity, is appropriately positioned to stabilize the gamma-phosphate in the transition state. The (betaalpha)4alpha fold of DhaM occurs a second time as a subfold in the DhaK subunit. By docking DhaL-ADP to this subfold, the nucleotide bound to DhaL and the C1-hydroxyl of Dha bound to DhaK are positioned for in-line transfer of phosphate. | ||
- | + | X-ray structures of the three Lactococcus lactis dihydroxyacetone kinase subunits and of a transient intersubunit complex.,Zurbriggen A, Jeckelmann JM, Christen S, Bieniossek C, Baumann U, Erni B J Biol Chem. 2008 Dec 19;283(51):35789-96. Epub 2008 Oct 28. PMID:18957416<ref>PMID:18957416</ref> | |
- | + | ||
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | < | + | </div> |
- | [[Category: Lactococcus lactis subsp. lactis | + | <div class="pdbe-citations 3ct4" style="background-color:#fffaf0;"></div> |
- | [[Category: Baumann | + | == References == |
- | [[Category: Christen | + | <references/> |
- | [[Category: Erni | + | __TOC__ |
- | [[Category: Jeckelmann | + | </StructureSection> |
- | [[Category: Zurbriggen | + | [[Category: Lactococcus lactis subsp. lactis]] |
- | + | [[Category: Large Structures]] | |
- | + | [[Category: Baumann U]] | |
- | + | [[Category: Christen S]] | |
- | + | [[Category: Erni B]] | |
- | + | [[Category: Jeckelmann JM]] | |
- | + | [[Category: Zurbriggen A]] |
Current revision
Structure of Dha-kinase subunit DhaK from L. Lactis
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