2qvl: Difference between revisions

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[[Image:2qvl.jpg|left|200px]]


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==Crystal Structure of Diacylglycerol Kinase==
The line below this paragraph, containing "STRUCTURE_2qvl", creates the "Structure Box" on the page.
<StructureSection load='2qvl' size='340' side='right'caption='[[2qvl]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2qvl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QVL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QVL FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#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=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
{{STRUCTURE_2qvl|  PDB=2qvl  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2qvl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qvl OCA], [https://pdbe.org/2qvl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qvl RCSB], [https://www.ebi.ac.uk/pdbsum/2qvl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qvl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DAGK_STAAR DAGK_STAAR] Catalyzes the phosphorylation of diacylglycerol (DAG) into phosphatidic acid. Is a key enzyme involved in the production of lipoteichoic acid by reintroducing DAG formed from the breakdown of membrane phospholipids into the phosphatidylglycerol biosynthetic pathway.<ref>PMID:17535816</ref>
== 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/qv/2qvl_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=2qvl ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Soluble diacylglycerol (DAG) kinases function as regulators of diacylglycerol metabolism in cell signaling and intermediary metabolism. We report the structure of a DAG kinase, DgkB from Staphylococcus aureus, both as the free enzyme and in complex with ADP. The molecule is a tight homodimer, and each monomer comprises two domains with the catalytic center located within the interdomain cleft. Two distinctive features of DkgB are a structural Mg2+ site and an associated Asp*water*Mg2+ network that extends toward the active site locale. Site-directed mutagenesis revealed that these features play important roles in the catalytic mechanism. The key active site residues and the components of the Asp*water*Mg2+ network are conserved in the catalytic cores of the mammalian signaling DAG kinases, indicating that these enzymes use the same mechanism and have similar structures as DgkB.


'''Crystal Structure of Diacylglycerol Kinase'''
Analysis of the Staphylococcus aureus DgkB structure reveals a common catalytic mechanism for the soluble diacylglycerol kinases.,Miller DJ, Jerga A, Rock CO, White SW Structure. 2008 Jul;16(7):1036-46. PMID:18611377<ref>PMID:18611377</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2qvl" style="background-color:#fffaf0;"></div>


==About this Structure==
==See Also==
2QVL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QVL OCA].
*[[Diacylglycerol kinase 3D structures|Diacylglycerol kinase 3D structures]]
[[Category: Diacylglycerol kinase]]
== References ==
[[Category: Single protein]]
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
[[Category: Jerga, A.]]
[[Category: Jerga A]]
[[Category: Miller, D J.]]
[[Category: Miller DJ]]
[[Category: Rock, C O.]]
[[Category: Rock CO]]
[[Category: White, S W.]]
[[Category: White SW]]
[[Category: Alpha-beta domain 1]]
[[Category: Beta sandwich domain 2]]
[[Category: Native protein]]
[[Category: Transferase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 18 12:04:10 2008''