1q57: Difference between revisions

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-[[Image:1q57.jpg|left|200px]]
- {{Structure
+==The Crystal Structure of the Bifunctional Primase-Helicase of Bacteriophage T7==
-|PDB= 1q57 |SIZE=350|CAPTION= <scene name='initialview01'>1q57</scene>, resolution 3.45&Aring;
+<StructureSection load='1q57' size='340' side='right'caption='[[1q57]], [[Resolution|resolution]] 3.45&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND=
+<table><tr><td colspan='2'>[[1q57]] is a 7 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=1Q57 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q57 FirstGlance]. <br>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.45&#8491;</td></tr>
-|GENE= 4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= Bacteriophage T7])
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1q57 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q57 OCA], [https://pdbe.org/1q57 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q57 RCSB], [https://www.ebi.ac.uk/pdbsum/1q57 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q57 ProSAT]</span></td></tr>
-}}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/HELIC_BPT7 HELIC_BPT7] ATP-dependent DNA helicase and primase essential for viral DNA replication and recombination (PubMed:21606333, PubMed:22977246, PubMed:32009150). The helicase moves 5' -> 3' on the lagging strand template, unwinding the DNA duplex ahead of the leading strand polymerase at the replication fork and generating ssDNA for both leading and lagging strand synthesis (PubMed:21606333, PubMed:22977246, PubMed:32009150). ATP or dTTP hydrolysis propels each helicase domain to translocate 2 nt per step sequentially along DNA (PubMed:30679383, PubMed:17604719). Mediates strand transfer when a joint molecule is available and participates in recombinational DNA repair through its role in strand exchange (PubMed:9096333, PubMed:8617248). Primase activity synthesizes short RNA primers at the sequence 5'-GTC-3' on the lagging strand that the polymerase elongates using dNTPs and providing the primase is still present (PubMed:6454135, PubMed:9139692).[HAMAP-Rule:MF_04154]<ref>PMID:17604719</ref> <ref>PMID:21606333</ref> <ref>PMID:22977246</ref> <ref>PMID:30679383</ref> <ref>PMID:32009150</ref> <ref>PMID:6454135</ref> <ref>PMID:8617248</ref> <ref>PMID:9096333</ref> <ref>PMID:9139692</ref>
+== 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/q5/1q57_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=1q57 ConSurf].
+<div style="clear:both"></div>
-'''The Crystal Structure of the Bifunctional Primase-Helicase of Bacteriophage T7'''
+==See Also==
+*[[RNA polymerase 3D structures|RNA polymerase 3D structures]]
+== References ==
-==Overview==
+<references/>
-Within minutes after infecting Escherichia coli, bacteriophage T7 synthesizes many copies of its genomic DNA. The lynchpin of the T7 replication system is a bifunctional primase-helicase that unwinds duplex DNA at the replication fork while initiating the synthesis of Okazaki fragments on the lagging strand. We have determined a 3.45 A crystal structure of the T7 primase-helicase that shows an articulated arrangement of the primase and helicase sites. The crystallized primase-helicase is a heptamer with a crown-like shape, reflecting an intimate packing of helicase domains into a ring that is topped with loosely arrayed primase domains. This heptameric isoform can accommodate double-stranded DNA in its central channel, which nicely explains its recently described DNA remodeling activity. The double-jointed structure of the primase-helicase permits a free range of motion for the primase and helicase domains that suggests how the continuous unwinding of DNA at the replication fork can be periodically coupled to Okazaki fragment synthesis.
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Escherichia phage T7]]
-Q57 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=1Q57 OCA].
+[[Category: Large Structures]]
+[[Category: Cheng Y]]
-==Reference==
+[[Category: Ellenberger T]]
-The crystal structure of the bifunctional primase-helicase of bacteriophage T7., Toth EA, Li Y, Sawaya MR, Cheng Y, Ellenberger T, Mol Cell. 2003 Nov;12(5):1113-23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14636571 14636571]
+[[Category: Li Y]]
-[[Category: Bacteriophage t7]]
+[[Category: Sawaya MR]]
-[[Category: Single protein]]
+[[Category: Toth EA]]
-[[Category: Cheng, Y.]]
-[[Category: Ellenberger, T.]]
-[[Category: Li, Y.]]
-[[Category: Sawaya, M R.]]
-[[Category: Toth, E A.]]
-[[Category: dna replication]]
-[[Category: dntpase]]
-[[Category: helicase]]
-[[Category: primase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:33:13 2008''