2pii: Difference between revisions

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 ==PII, GLNB PRODUCT==
-<StructureSection load='2pii' size='340' side='right' caption='[[2pii]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+<StructureSection load='2pii' size='340' side='right'caption='[[2pii]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2pii]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PII OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PII FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2pii]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PII OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PII FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GLNB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2pii FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pii OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2pii RCSB], [http://www.ebi.ac.uk/pdbsum/2pii PDBsum]</span></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=2pii FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pii OCA], [https://pdbe.org/2pii PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pii RCSB], [https://www.ebi.ac.uk/pdbsum/2pii PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pii ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/GLNB_ECOLI GLNB_ECOLI] P-II indirectly controls the transcription of the glutamine synthetase gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of GlnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase by GlnE, so activating the enzyme.
 == 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/pi/2pii_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pi/2pii_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=2pii ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The structure of the bacterial signal transduction protein P(II) has been refined to an R factor of 13.2% using 3sigma data between 10 and 1.9 A. The crystals exhibited twinning by merohedry and X-ray intensities were corrected using the method of Fisher &amp; Sweet [Fisher &amp; Sweet (1980). Acta Cryst. A36, 755-760] prior to refinement. Our earlier 2.7 A structure [Cheah, Carr, Suffolk, Vasudevan, Dixon &amp; Ollis (1994). Structure, 2, 981-990] served as a starting model. P(II) is a trimeric molecule, each subunit has a mass of 12.4 kDa and contains 112 amino-acid residues. The refined model includes all 1065 protein atoms per subunit plus 312 water molecules. The high-resolution refinement confirms the correctness of our 2.7 A model, although it leads to a redefinition of the extent of various secondary-structural elements. The monomeric structure of P(II) exhibits an interlocking double betaalphabeta fold. This is a stable fold found in a number of proteins with diverse functions. The association of the protein into a trimer leads to a new structure which we describe in detail. The effects of crystal packing forces are discussed and potential interaction sites with other proteins and effector molecules are identified.
-X-ray structure of the signal transduction protein from Escherichia coli at 1.9 A.,Carr PD, Cheah E, Suffolk PM, Vasudevan SG, Dixon NE, Ollis DL Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):93-104. PMID:15299730<ref>PMID:15299730</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[Category: Escherichia coli]]
-[[Category: Carr, P D.]]
+[[Category: Large Structures]]
-[[Category: Cheah, E.]]
+[[Category: Carr PD]]
-[[Category: Ollis, D L.]]
+[[Category: Cheah E]]
-[[Category: Suffolk, P M.]]
+[[Category: Ollis DL]]
-[[Category: Signal transduction protein]]
+[[Category: Suffolk PM]]