1ro0

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{{Seed}}
 
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[[Image:1ro0.png|left|200px]]
 
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==Bifunctional DNA primase/polymerase domain of ORF904 from the archaeal plasmid pRN1- Triple mutant F50M/L107M/L110M SeMet remote==
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The line below this paragraph, containing "STRUCTURE_1ro0", creates the "Structure Box" on the page.
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<StructureSection load='1ro0' size='340' side='right'caption='[[1ro0]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1ro0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfolobus_islandicus Sulfolobus islandicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RO0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RO0 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_1ro0| PDB=1ro0 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ro0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ro0 OCA], [https://pdbe.org/1ro0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ro0 RCSB], [https://www.ebi.ac.uk/pdbsum/1ro0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ro0 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q54324_SULIS Q54324_SULIS]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ro/1ro0_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1ro0 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Genome replication generally requires primases, which synthesize an initial oligonucleotide primer, and DNA polymerases, which elongate the primer. Primase and DNA polymerase activities are combined, however, in newly identified replicases from archaeal plasmids, such as pRN1 from Sulfolobus islandicus. Here we present a structure-function analysis of the pRN1 primase-polymerase (prim-pol) domain. The crystal structure shows a central depression lined by conserved residues. Mutations on one side of the depression reduce DNA affinity. On the opposite side of the depression cluster three acidic residues and a histidine, which are required for primase and DNA polymerase activity. One acidic residue binds a manganese ion, suggestive of a metal-dependent catalytic mechanism. The structure does not show any similarity to DNA polymerases, but is distantly related to archaeal and eukaryotic primases, with corresponding active-site residues. We propose that archaeal and eukaryotic primases and the prim-pol domain have a common evolutionary ancestor, a bifunctional replicase for small DNA genomes.
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===Bifunctional DNA primase/polymerase domain of ORF904 from the archaeal plasmid pRN1- Triple mutant F50M/L107M/L110M SeMet remote===
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Structure of a bifunctional DNA primase-polymerase.,Lipps G, Weinzierl AO, von Scheven G, Buchen C, Cramer P Nat Struct Mol Biol. 2004 Feb;11(2):157-62. Epub 2004 Jan 18. PMID:14730355<ref>PMID:14730355</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_14730355}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1ro0" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 14730355 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_14730355}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1RO0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_islandicus Sulfolobus islandicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RO0 OCA].
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==Reference==
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Structure of a bifunctional DNA primase-polymerase., Lipps G, Weinzierl AO, von Scheven G, Buchen C, Cramer P, Nat Struct Mol Biol. 2004 Feb;11(2):157-62. Epub 2004 Jan 18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14730355 14730355]
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[[Category: Single protein]]
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[[Category: Sulfolobus islandicus]]
[[Category: Sulfolobus islandicus]]
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[[Category: Buchen, C.]]
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[[Category: Buchen C]]
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[[Category: Cramer, P.]]
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[[Category: Cramer P]]
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[[Category: Lipps, G.]]
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[[Category: Lipps G]]
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[[Category: Scheven, G von.]]
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[[Category: Weinzierl AO]]
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[[Category: Weinzierl, A O.]]
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[[Category: Von Scheven G]]
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[[Category: Dna polymerase]]
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[[Category: Evolution of nucleic acid polymerizing enzyme]]
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[[Category: Polymerization]]
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[[Category: Primase]]
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[[Category: Replication]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:49:51 2008''
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Current revision

Bifunctional DNA primase/polymerase domain of ORF904 from the archaeal plasmid pRN1- Triple mutant F50M/L107M/L110M SeMet remote

PDB ID 1ro0

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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