1un8

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{{Seed}}
 
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[[Image:1un8.png|left|200px]]
 
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==Crystal structure of the dihydroxyacetone kinase of C. freundii (native form)==
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The line below this paragraph, containing "STRUCTURE_1un8", creates the "Structure Box" on the page.
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<StructureSection load='1un8' size='340' side='right'caption='[[1un8]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1un8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Citrobacter_freundii Citrobacter freundii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UN8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UN8 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.5&#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=MYY:(2R)-3-(PHOSPHONOOXY)-2-(TETRADECANOYLOXY)PROPYL+PALMITATE'>MYY</scene></td></tr>
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{{STRUCTURE_1un8| PDB=1un8 | SCENE= }}
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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=1un8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1un8 OCA], [https://pdbe.org/1un8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1un8 RCSB], [https://www.ebi.ac.uk/pdbsum/1un8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1un8 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DHAK_CITFR DHAK_CITFR] Catalyzes the phosphorylation 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/un/1un8_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=1un8 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Dihydroxyacetone kinases are a sequence-conserved family of enzymes, which utilize two different phosphoryldonors, ATP in animals, plants and some bacteria, and a multiphosphoprotein of the phosphoenolpyruvate carbohydrate phosphotransferase system in bacteria. Here we report the 2.5-A crystal structure of the homodimeric Citrobacter freundii dihydroxyacetone kinase complex with an ATP analogue and dihydroxyacetone. The N-terminal domain consists of two alpha/beta-folds with a molecule of dihydroxyacetone covalently bound in hemiaminal linkage to the N epsilon 2 of His-220. The C-terminal domain consists of a regular eight-helix alpha-barrel. The eight helices form a deep pocket, which includes a tightly bound phospholipid. Only the lipid headgroup protrudes from the surface. The nucleotide is bound on the top of the barrel across from the entrance to the lipid pocket. The phosphate groups are coordinated by two Mg2+ ions to gamma-carboxyl groups of aspartyl residues. The ATP binding site does not contain positively charged or aromatic groups. Paralogues of dihydroxyacetone kinase also occur in association with transcription regulators and proteins of unknown function pointing to biological roles beyond triose metabolism.
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===CRYSTAL STRUCTURE OF THE DIHYDROXYACETONE KINASE OF C. FREUNDII (NATIVE FORM)===
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Crystal structure of the Citrobacter freundii dihydroxyacetone kinase reveals an eight-stranded alpha-helical barrel ATP-binding domain.,Siebold C, Arnold I, Garcia-Alles LF, Baumann U, Erni B J Biol Chem. 2003 Nov 28;278(48):48236-44. Epub 2003 Sep 9. PMID:12966101<ref>PMID:12966101</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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The line below this paragraph, {{ABSTRACT_PUBMED_12966101}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1un8" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 12966101 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_12966101}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1UN8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Citrobacter_freundii Citrobacter freundii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UN8 OCA].
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==Reference==
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Crystal structure of the Citrobacter freundii dihydroxyacetone kinase reveals an eight-stranded alpha-helical barrel ATP-binding domain., Siebold C, Arnold I, Garcia-Alles LF, Baumann U, Erni B, J Biol Chem. 2003 Nov 28;278(48):48236-44. Epub 2003 Sep 9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12966101 12966101]
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[[Category: Citrobacter freundii]]
[[Category: Citrobacter freundii]]
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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: Arnold I]]
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[[Category: Arnold, I.]]
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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 LF]]
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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: Dha kinase]]
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[[Category: Dihydroxyacetone kinase]]
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[[Category: Kinase,glycerone kinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:02:34 2008''
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Current revision

Crystal structure of the dihydroxyacetone kinase of C. freundii (native form)

PDB ID 1un8

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