3q83: Difference between revisions

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-[[Image:3q83.jpg|left|200px]]
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+==Crystal structure of Staphylococcus aureus nucleoside diphosphate kinase==
-The line below this paragraph, containing "STRUCTURE_3q83", creates the "Structure Box" on the page.
+<StructureSection load='3q83' size='340' side='right'caption='[[3q83]], [[Resolution|resolution]] 2.50&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'>[[3q83]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_COL Staphylococcus aureus subsp. aureus COL]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q83 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3Q83 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]] 2.5&#8491;</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=3q83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q83 OCA], [https://pdbe.org/3q83 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3q83 RCSB], [https://www.ebi.ac.uk/pdbsum/3q83 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3q83 ProSAT]</span></td></tr>
-{{STRUCTURE_3q83|  PDB=3q83  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/NDK_STAAC NDK_STAAC] Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate (By similarity).
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Nucleoside diphosphate kinases (NDK) are characterized by high catalytic turnover rates and diverse substrate specificity. These features make this enzyme an effective activator of a pro-drug-an application that has been actively pursued for a variety of therapeutic strategies. The catalytic mechanism of this enzyme is governed by a conserved histidine that coordinates a magnesium ion at the active site. Despite substantial structural and biochemical information on NDK, the mechanistic feature of the phospho-transfer that leads to auto-phosphorylation remains unclear. While the role of the histidine residue is well documented, the other active site residues, in particular the conserved serine remains poorly characterized. Studies on some homologues suggest no role for the serine residue at the active site, while others suggest a crucial role for this serine in the regulation and quaternary association of this enzyme in some species. Here we report the biochemical features of the Staphylococcus aureus NDK and the mutant enzymes. We also describe the crystal structures of the apo-NDK, as a transition state mimic with vanadate and in complex with different nucleotide substrates. These structures formed the basis for molecular dynamics simulations to understand the broad substrate specificity of this enzyme and the role of active site residues in the phospho-transfer mechanism and oligomerization. Put together, these data suggest that concerted changes in the conformation of specific residues facilitate the stabilization of nucleotide complexes thereby enabling the steps involved in the ping-pong reaction mechanism without large changes to the overall structure of this enzyme.
-===Crystal structure of Staphylococcus aureus nucleoside diphosphate kinase===
+Conformational basis for substrate recognition and regulation of catalytic activity in Staphylococcus aureus nucleoside di-phosphate kinase.,Srivastava SK, Rajasree K, Gopal B Biochim Biophys Acta. 2011 Jun 27. PMID:21745603<ref>PMID:21745603</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3q83" style="background-color:#fffaf0;"></div>
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+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_21745603}}, adds the Publication Abstract to the page
+*[[Nucleoside diphosphate kinase 3D structures|Nucleoside diphosphate kinase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 21745603 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_21745603}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-[[3q83]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus Staphylococcus aureus subsp. aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q83 OCA].
+[[Category: Staphylococcus aureus subsp. aureus COL]]
+[[Category: Gopal B]]
-==Reference==
+[[Category: Rajasree K]]
-<ref group="xtra">PMID:021745603</ref><references group="xtra"/>
+[[Category: Srivastava SK]]
-[[Category: Nucleoside-diphosphate kinase]]
-[[Category: Staphylococcus aureus subsp. aureus]]
-[[Category: Gopal, B.]]
-[[Category: Rajasree, K.]]
-[[Category: Srivastava, S K.]]
-[[Category: Alpha-beta protein family]]
-[[Category: Ferridoxin fold]]
-[[Category: Kinase]]
-[[Category: Metal binding]]
-[[Category: Nucleotide binding]]
-[[Category: Nucleotide metabolism]]
-[[Category: Phosphorylation]]
-[[Category: Transferase]]