1s77: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1s77.gif|left|200px]]
- {{Structure
+==T7 RNAP product pyrophosphate elongation complex==
-|PDB= 1s77 |SIZE=350|CAPTION= <scene name='initialview01'>1s77</scene>, resolution 2.69&Aring;
+<StructureSection load='1s77' size='340' side='right'caption='[[1s77]], [[Resolution|resolution]] 2.69&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=POP:PYROPHOSPHATE 2-'>POP</scene>
+<table><tr><td colspan='2'>[[1s77]] is a 4 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=1S77 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S77 FirstGlance]. <br>
-|ACTIVITY= [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]
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.69&#8491;</td></tr>
-|GENE= 1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= Bacteriophage T7])
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3DA:3-DEOXYADENOSINE-5-MONOPHOSPHATE'>3DA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</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=1s77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s77 OCA], [https://pdbe.org/1s77 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s77 RCSB], [https://www.ebi.ac.uk/pdbsum/1s77 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s77 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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/s7/1s77_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=1s77 ConSurf].
+<div style="clear:both"></div>
-'''T7 RNAP product pyrophosphate elongation complex'''
+==See Also==
+*[[RNA polymerase 3D structures|RNA polymerase 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-RNA polymerase functions like a molecular motor that can convert chemical energy into the work of strand separation and translocation along the DNA during transcription. The structures of phage T7 RNA polymerase in an elongation phase substrate complex that includes the incoming nucleoside triphosphate and a pretranslocation product complex that includes the product pyrophosphate (PPi) are described here. These structures and the previously determined posttranslocation elongation complex demonstrate that two enzyme conformations exist during a cycle of single nucleotide addition. One orientation of a five-helix subdomain is stabilized by the phosphates of either the incoming NTP or by the product PPi. A second orientation of this subdomain is stable in their absence and is associated with translocation of the heteroduplex product as well as strand separation of the downstream DNA. We propose that the dissociation of the product PPi after nucleotide addition produces the protein conformational change resulting in translocation and strand separation.
+[[Category: Escherichia phage T7]]
+[[Category: Large Structures]]
-==About this Structure==
+[[Category: Steitz TA]]
-S77 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t7 Bacteriophage t7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S77 OCA].
+[[Category: Yin YW]]
-==Reference==
-The structural mechanism of translocation and helicase activity in T7 RNA polymerase., Yin YW, Steitz TA, Cell. 2004 Feb 6;116(3):393-404. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15016374 15016374]
-[[Category: Bacteriophage t7]]
-[[Category: DNA-directed RNA polymerase]]
-[[Category: Single protein]]
-[[Category: Steitz, T A.]]
-[[Category: Yin, Y W.]]
-[[Category: MG]]
-[[Category: POP]]
-[[Category: t7 rna polymerase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:01:25 2008''