1g71: Difference between revisions

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-[[Image:1g71.gif|left|200px]]
- {{Structure
+==CRYSTAL STRUCTURE OF PYROCOCCUS FURIOSUS DNA PRIMASE==
-|PDB= 1g71 |SIZE=350|CAPTION= <scene name='initialview01'>1g71</scene>, resolution 2.3&Aring;
+<StructureSection load='1g71' size='340' side='right'caption='[[1g71]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
+<table><tr><td colspan='2'>[[1g71]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G71 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G71 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]] 2.3&#8491;</td></tr>
-|GENE=
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1g71 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g71 OCA], [https://pdbe.org/1g71 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g71 RCSB], [https://www.ebi.ac.uk/pdbsum/1g71 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g71 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PRIS_PYRFU PRIS_PYRFU] Catalytic subunit of DNA primase, an RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. The small subunit contains the primase catalytic core and has DNA synthesis activity on its own. Binding to the large subunit stabilizes and modulates the activity, increasing the rate of DNA synthesis while decreasing the length of the DNA fragments, and conferring RNA synthesis capability. The DNA polymerase activity may enable DNA primase to also catalyze primer extension after primer synthesis. May also play a role in DNA repair.<ref>PMID:11584001</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/g7/1g71_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=1g71 ConSurf].
+<div style="clear:both"></div>
-'''CRYSTAL STRUCTURE OF PYROCOCCUS FURIOSUS DNA PRIMASE'''
+==See Also==
+*[[RNA polymerase 3D structures|RNA polymerase 3D structures]]
+== References ==
-==Overview==
+<references/>
-Primases are essential components of the DNA replication apparatus in every organism. They catalyze the synthesis of oligoribonucleotides on single-stranded DNA, which subsequently serve as primers for the replicative DNA polymerases. In contrast to bacterial primases, the archaeal enzymes are closely related to their eukaryotic counterparts. We have solved the crystal structure of the catalytic primase subunit from the hyperthermophilic archaeon Pyrococcus furiosus at 2.3 A resolution by multiwavelength anomalous dispersion methods. The structure shows a two-domain arrangement with a novel zinc knuckle motif located in the primase (prim) domain. In this first structure of a complete protein of the archaeal/eukaryotic primase family, the arrangement of the catalytically active residues resembles the active sites of various DNA polymerases that are unrelated in fold.
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-G71 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G71 OCA].
-==Reference==
-Crystal structure of a DNA-dependent RNA polymerase (DNA primase)., Augustin MA, Huber R, Kaiser JT, Nat Struct Biol. 2001 Jan;8(1):57-61. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11135672 11135672]
 [[Category: Pyrococcus furiosus]]
-[[Category: Single protein]]
+[[Category: Augustin MA]]
-[[Category: Augustin, M A.]]
+[[Category: Huber R]]
-[[Category: Huber, R.]]
+[[Category: Kaiser JT]]
-[[Category: Kaiser, J T.]]
-[[Category: CL]]
-[[Category: SO4]]
-[[Category: ZN]]
-[[Category: zinc-knuckle]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:19:06 2008''