1ghh: Difference between revisions

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-{{Seed}}
-[[Image:1ghh.png|left|200px]]
-<!--
+==SOLUTION STRUCTURE OF DINI==
-The line below this paragraph, containing "STRUCTURE_1ghh", creates the "Structure Box" on the page.
+<StructureSection load='1ghh' size='340' side='right'caption='[[1ghh]]' 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'>[[1ghh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1f0a 1f0a]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GHH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GHH 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">Solution NMR</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=1ghh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ghh OCA], [https://pdbe.org/1ghh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ghh RCSB], [https://www.ebi.ac.uk/pdbsum/1ghh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ghh ProSAT]</span></td></tr>
-{{STRUCTURE_1ghh|  PDB=1ghh  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/DINI_ECOLI DINI_ECOLI] Involved in SOS regulation. Inhibits RecA by preventing RecA to bind ssDNA. Can displace ssDNA from RecA.
+== 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/gh/1ghh_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/main_output.php?pdb_ID=1ghh ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The Escherichia coli RecA protein triggers both DNA repair and mutagenesis in a process known as the SOS response. The 81-residue E. coli protein DinI inhibits activity of RecA in vivo. The solution structure of DinI has been determined by multidimensional triple resonance NMR spectroscopy, using restraints derived from two sets of residual dipolar couplings, obtained in bicelle and phage media, supplemented with J couplings and a moderate number of NOE restraints. DinI has an alpha/beta fold comprised of a three-stranded beta-sheet and two alpha-helices. The beta-sheet topology is unusual: the central strand is flanked by a parallel and an antiparallel strand and the sheet is remarkably flat. The structure of DinI shows that six negatively charged Glu and Asp residues on DinI's kinked C-terminal alpha-helix form an extended, negatively charged ridge. We propose that this ridge mimics the electrostatic character of the DNA phospodiester backbone, thereby enabling DinI to compete with single-stranded DNA for RecA binding. Biochemical data confirm that DinI is able to displace ssDNA from RecA.
-===SOLUTION STRUCTURE OF DINI===
+Solution structure of DinI provides insight into its mode of RecA inactivation.,Ramirez BE, Voloshin ON, Camerini-Otero RD, Bax A Protein Sci. 2000 Nov;9(11):2161-9. PMID:11152126<ref>PMID:11152126</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_11152126}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1ghh" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 11152126 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_11152126}}
+__TOC__
+</StructureSection>
-==About this Structure==
-GHH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1f0a 1f0a]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GHH OCA].
-==Reference==
-Solution structure of DinI provides insight into its mode of RecA inactivation., Ramirez BE, Voloshin ON, Camerini-Otero RD, Bax A, Protein Sci. 2000 Nov;9(11):2161-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11152126 11152126]
 [[Category: Escherichia coli]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Bax, A.]]
+[[Category: Bax A]]
-[[Category: Camerini-Otero, R D.]]
+[[Category: Camerini-Otero RD]]
-[[Category: Ramirez, B E.]]
+[[Category: Ramirez BE]]
-[[Category: Voloshin, O N.]]
+[[Category: Voloshin ON]]
-[[Category: Bicelle]]
-[[Category: Dini]]
-[[Category: Dipolar coupling]]
-[[Category: Liquid crystal]]
-[[Category: Nmr]]
-[[Category: Pf1]]
-[[Category: Reca]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 05:17:40 2008''