2jgv: Difference between revisions

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-{{Seed}}
-[[Image:2jgv.png|left|200px]]
-<!--
+==STRUCTURE OF Staphylococcus aureus D-TAGATOSE-6-PHOSPHATE KINASE in complex with ADP==
-The line below this paragraph, containing "STRUCTURE_2jgv", creates the "Structure Box" on the page.
+<StructureSection load='2jgv' size='340' side='right'caption='[[2jgv]], [[Resolution|resolution]] 2.00&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'>[[2jgv]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_NCTC_8325 Staphylococcus aureus subsp. aureus NCTC 8325]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JGV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JGV 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&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-{{STRUCTURE_2jgv|  PDB=2jgv  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2jgv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jgv OCA], [https://pdbe.org/2jgv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jgv RCSB], [https://www.ebi.ac.uk/pdbsum/2jgv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jgv ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/LACC_STAA8 LACC_STAA8]
+== 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/jg/2jgv_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=2jgv ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+High resolution structures of Staphylococcus aureus d-tagatose-6-phosphate kinase (LacC) in two crystal forms are herein reported. The structures define LacC in apoform, in binary complexes with ADP or the co-factor analogue AMP-PNP, and in a ternary complex with AMP-PNP and D-tagatose-6-phosphate. The tertiary structure of the LacC monomer, which is closely related to other members of the pfkB subfamily of carbohydrate kinases, is composed of a large alpha/beta core domain and a smaller, largely beta "lid." Four extended polypeptide segments connect these two domains. Dimerization of LacC occurs via interactions between lid domains, which come together to form a beta-clasp structure. Residues from both subunits contribute to substrate binding. LacC adopts a closed structure required for phosphoryl transfer only when both substrate and co-factor are bound. A reaction mechanism similar to that used by other phosphoryl transferases is proposed, although unusually, when both substrate and co-factor are bound to the enzyme two Mg(2+) ions are observed in the active site. A new motif of amino acid sequence conservation common to the pfkB subfamily of carbohydrate kinases is identified.
-===STRUCTURE OF STAPHYLOCOCCUS AUREUS D-TAGATOSE-6-PHOSPHATE KINASE IN COMPLEX WITH ADP===
+Structures of Staphylococcus aureus D-tagatose-6-phosphate kinase implicate domain motions in specificity and mechanism.,Miallau L, Hunter WN, McSweeney SM, Leonard GA J Biol Chem. 2007 Jul 6;282(27):19948-57. Epub 2007 Apr 25. PMID:17459874<ref>PMID:17459874</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_17459874}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 2jgv" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 17459874 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_17459874}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-JGV 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=2JGV OCA].
+[[Category: Staphylococcus aureus subsp. aureus NCTC 8325]]
+[[Category: Hunter WN]]
-==Reference==
+[[Category: Leonard GA]]
-Structures of Staphylococcus aureus D-tagatose-6-phosphate kinase implicate domain motions in specificity and mechanism., Miallau L, Hunter WN, McSweeney SM, Leonard GA, J Biol Chem. 2007 Jul 6;282(27):19948-57. Epub 2007 Apr 25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17459874 17459874]
+[[Category: McSweeney SM]]
-[[Category: Single protein]]
+[[Category: Miallau L]]
-[[Category: Staphylococcus aureus]]
-[[Category: Tagatose-6-phosphate kinase]]
-[[Category: Hunter, W N.]]
-[[Category: Leonard, G A.]]
-[[Category: Mcsweeney, S M.]]
-[[Category: Miallau, L.]]
-[[Category: Conformational change]]
-[[Category: D-tagatose-6-phosphate kinase]]
-[[Category: Kinase]]
-[[Category: Lactose metabolism]]
-[[Category: Phosphoryl transfer]]
-[[Category: Transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:47:31 2008''