1aro: Difference between revisions

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 ==T7 RNA POLYMERASE COMPLEXED WITH T7 LYSOZYME==
-<StructureSection load='1aro' size='340' side='right' caption='[[1aro]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
+<StructureSection load='1aro' size='340' side='right'caption='[[1aro]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1aro]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpt7 Bpt7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ARO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ARO FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1aro]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_phage_T7 Escherichia phage T7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ARO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ARO FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</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]] 2.8&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">T7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10760 BPT7])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_RNA_polymerase DNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.6 2.7.7.6] </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=1aro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aro OCA], [https://pdbe.org/1aro PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aro RCSB], [https://www.ebi.ac.uk/pdbsum/1aro PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aro ProSAT]</span></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=1aro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aro OCA], [http://pdbe.org/1aro PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1aro RCSB], [http://www.ebi.ac.uk/pdbsum/1aro PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1aro ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/RPOL_BPT7 RPOL_BPT7]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of the late genes of T7. It is rifampicin-resistant. It recognizes a specific promoter sequence, unwinds the double-stranded RNA to expose the coding strand for templating, initiates transcription preferentially with a purine. [[http://www.uniprot.org/uniprot/ENLYS_BPT7 ENLYS_BPT7]] Plays an important role in the switch between viral transcription and T7 genome replication. Once produced in sufficient amount, interacts with and inhibits T7 RNA polymerase that becomes unable to produce additional transcripts. This lysozyme-polymerase complex in turn plays an active role in T7 genome replication and packaging.  Endolysin with amidase activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and breaking down the peptidoglycan layer.
+[https://www.uniprot.org/uniprot/RPOL_BPT7 RPOL_BPT7] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of the late genes of T7. It is rifampicin-resistant. It recognizes a specific promoter sequence, unwinds the double-stranded RNA to expose the coding strand for templating, initiates transcription preferentially with a purine.
 == 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/ar/1aro_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ar/1aro_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 21: / 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=1aro ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The T7 RNA polymerase-T7 lysozyme complex regulates phage gene expression during infection of Escherichia coli. The 2.8 A crystal structure of the complex reveals that lysozyme binds at a site remote from the polymerase active site, suggesting an indirect mechanism of inhibition. Comparison of the T7 RNA polymerase structure with that of the homologous pol I family of DNA polymerases reveals identities in the catalytic site but also differences specific to RNA polymerase function. The structure of T7 RNA polymerase presented here differs significantly from a previously published structure. Sequence similarities between phage RNA polymerases and those from mitochondria and chloroplasts, when interpreted in the context of our revised model of T7 RNA polymerase, suggest a conserved fold.
-Structure of T7 RNA polymerase complexed to the transcriptional inhibitor T7 lysozyme.,Jeruzalmi D, Steitz TA EMBO J. 1998 Jul 15;17(14):4101-13. PMID:9670025<ref>PMID:9670025</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1aro" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Lysozyme 3D structures|Lysozyme 3D structures]]
-== References ==
+*[[RNA polymerase 3D structures|RNA polymerase 3D structures]]
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Bpt7]]
+[[Category: Escherichia phage T7]]
-[[Category: DNA-directed RNA polymerase]]
+[[Category: Large Structures]]
-[[Category: Jeruzalmi, D]]
+[[Category: Jeruzalmi D]]
-[[Category: Steitz, T]]
+[[Category: Steitz T]]
-[[Category: Dna-directed rna polymerase]]
-[[Category: Glycosidase]]
-[[Category: Hydrolase]]
-[[Category: Transcription]]