1eyv: Difference between revisions

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OCA

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 ==THE CRYSTAL STRUCTURE OF NUSB FROM MYCOBACTERIUM TUBERCULOSIS==
-<StructureSection load='1eyv' size='340' side='right' caption='[[1eyv]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
+<StructureSection load='1eyv' size='340' side='right'caption='[[1eyv]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1eyv]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EYV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EYV FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1eyv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EYV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EYV FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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]] 1.6&#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=1eyv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eyv OCA], [http://pdbe.org/1eyv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1eyv RCSB], [http://www.ebi.ac.uk/pdbsum/1eyv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1eyv ProSAT], [http://www.topsan.org/Proteins/TBSGC/1eyv TOPSAN]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=1eyv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eyv OCA], [https://pdbe.org/1eyv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eyv RCSB], [https://www.ebi.ac.uk/pdbsum/1eyv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eyv ProSAT], [https://www.topsan.org/Proteins/TBSGC/1eyv TOPSAN]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/NUSB_MYCTU NUSB_MYCTU]] Involved in the transcription termination process (By similarity).
+[https://www.uniprot.org/uniprot/NUSB_MYCTU NUSB_MYCTU] Involved in the transcription termination process (By similarity).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 19: / Line 20: @@
 </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=1eyv ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Both prokaryotes and eukaryotes regulate transcription through mechanisms that suppress termination signals. An antitermination mechanism was first characterized in bacteriophage lambda. Bacteria have analogous machinery that regulates ribosomal RNA transcription and employs host factors, called the N-utilizing (where N stands for the phage lambda N protein) substances (Nus), NusA, NusB, NusE and NusG. Here we report the crystal structure of NusB from Mycobacterium tuberculosis, the bacterium that causes tuberculosis in humans. This molecule shares a similar tertiary structure with the related Escherichia coli protein but adopts a different quaternary organization. We show that, unlike the E. coli homolog, M. tuberculosis NusB is dimeric both in solution and in the crystal. These data help provide a framework for understanding the structural and biological function of NusB in the prokaryotic transcriptional antitermination complex.
-The crystal structure of NusB from Mycobacterium tuberculosis.,Gopal B, Haire LF, Cox RA, Jo Colston M, Major S, Brannigan JA, Smerdon SJ, Dodson G Nat Struct Biol. 2000 Jun;7(6):475-8. PMID:10881194<ref>PMID:10881194</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1eyv" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Brannigan, J A]]
+[[Category: Large Structures]]
-[[Category: Colston, M J]]
+[[Category: Mycobacterium tuberculosis]]
-[[Category: Cox, R A]]
+[[Category: Brannigan JA]]
-[[Category: Dodson, G G]]
+[[Category: Colston MJ]]
-[[Category: Gopal, B]]
+[[Category: Cox RA]]
-[[Category: Haire, L F]]
+[[Category: Dodson GG]]
-[[Category: Major, S]]
+[[Category: Gopal B]]
-[[Category: Smerdon, S J]]
+[[Category: Haire LF]]
-[[Category: Structural genomic]]
+[[Category: Major S]]
-[[Category: Helical bundle]]
+[[Category: Smerdon SJ]]
-[[Category: PSI, Protein structure initiative]]
-[[Category: Tbsgc]]
-[[Category: Transcription]]