1neq: Difference between revisions

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-{{Seed}}
-[[Image:1neq.png|left|200px]]
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+==SOLUTION STRUCTURE OF THE MU NER PROTEIN BY MULTIDIMENSIONAL NMR==
-The line below this paragraph, containing "STRUCTURE_1neq", creates the "Structure Box" on the page.
+<StructureSection load='1neq' size='340' side='right'caption='[[1neq]]' 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'>[[1neq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_Mu Escherichia virus Mu]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NEQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NEQ 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=1neq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1neq OCA], [https://pdbe.org/1neq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1neq RCSB], [https://www.ebi.ac.uk/pdbsum/1neq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1neq ProSAT]</span></td></tr>
-{{STRUCTURE_1neq|  PDB=1neq  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/NER_BPMU NER_BPMU] Negative regulator of transcription starting from the Pe and Pc promoters of Mu. Also negatively regulates its own gene transcription.
+== 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/ne/1neq_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=1neq ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+BACKGROUND: The Mu Ner protein is a small (74 amino acids), basic, DNA-binding protein found in phage Mu. It belongs to a class of proteins, the cro and repressor proteins, that regulate the switch from the lysogenic to the lytic state of the phage life cycle. There is no significant sequence identity between Mu Ner and the cro proteins of other phages, despite their functional similarity. In addition, there is no significant sequence identity with any other DNA-binding proteins, with the exception of Ner from the related phage D108 and the Nlp protein of Escherichia coli. As the tertiary structures of Mu Ner and these two related proteins are unknown, it is clear that a three-dimensional (3D) structure of Mu Ner is essential in order to gain insight into its mode of DNA binding. RESULTS: The 3D solution structure of Mu Ner has been solved by 3D and 4D heteronuclear magnetic resonance spectroscopy. The structure consists of five alpha helices, two of which comprise a helix-turn-helix (HTH) motif. Analysis of line broadening and disappearance of crosspeaks in a 1H-15N correlation spectrum of the Mu Ner-DNA complex suggests that residues in these two helices are most likely to be in contact with the DNA. CONCLUSIONS: Like the functionally analogous cro proteins from phages lambda and 434, the Mu Ner protein possesses a HTH DNA recognition motif. The Ner protein from phage D108 and the Nlp protein from E. coli are likely to have very similar tertiary structures due to high amino-acid-sequence identity with Mu Ner.
-===SOLUTION STRUCTURE OF THE MU NER PROTEIN BY MULTIDIMENSIONAL NMR===
+The solution structure of the Mu Ner protein reveals a helix-turn-helix DNA recognition motif.,Strzelecka TE, Clore GM, Gronenborn AM Structure. 1995 Oct 15;3(10):1087-95. PMID:8590003<ref>PMID:8590003</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_8590003}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1neq" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 8590003 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_8590003}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Escherichia virus Mu]]
-NEQ is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_mu Enterobacteria phage mu]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NEQ OCA].
+[[Category: Large Structures]]
+[[Category: Clore GM]]
-==Reference==
+[[Category: Gronenborn AM]]
-<ref group="xtra">PMID:8590003</ref><references group="xtra"/>
+[[Category: Strzelecka TE]]
-[[Category: Enterobacteria phage mu]]
-[[Category: Clore, G M.]]
-[[Category: Gronenborn, A M.]]
-[[Category: Strzelecka, T E.]]
-[[Category: Dna-binding protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 16:55:06 2009''