2qvl

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "2qvl" [edit=sysop:move=sysop])
Current revision (08:35, 30 October 2024) (edit) (undo)
 
(5 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2qvl.png|left|200px]]
 
-
{{STRUCTURE_2qvl| PDB=2qvl | SCENE= }}
+
==Crystal Structure of Diacylglycerol Kinase==
 +
<StructureSection load='2qvl' size='340' side='right'caption='[[2qvl]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 +
== Structural highlights ==
 +
<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>
 +
</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>
 +
<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>
 +
<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>
-
{{ABSTRACT_PUBMED_18611377}}
+
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 1 chain structure with 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]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
<ref group="xtra">PMID:018611377</ref><references group="xtra"/>
+
__TOC__
-
[[Category: Diacylglycerol kinase]]
+
</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]]
+

Current revision

Crystal Structure of Diacylglycerol Kinase

PDB ID 2qvl

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2qvl"
Personal tools