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1zt2

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(New page: 200px<br /><applet load="1zt2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zt2, resolution 3.33&Aring;" /> '''Heterodimeric struct...)
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[[Image:1zt2.gif|left|200px]]<br /><applet load="1zt2" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1zt2, resolution 3.33&Aring;" />
 
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'''Heterodimeric structure of the core primase.'''<br />
 
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==Overview==
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==Heterodimeric structure of the core primase.==
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Primases are DNA-dependent RNA polymerases that synthesize the, oligoribonucleotide primers essential to DNA replication. In archaeal and, eukaryotic organisms, the core primase is a heterodimeric enzyme composed, of a small and a large subunit. Here we report a crystallographic and, biochemical analysis of the core primase from the archaeon Sulfolobus, solfataricus. The structure provides the first three-dimensional, description of the large subunit and its interaction with the small, subunit. The evolutionary conservation of amino acids at the, protein-protein interface implies that the observed mode of subunit, association is conserved among archaeal and eukaryotic primases. The, orientation of the large subunit in the core primase probably excludes its, direct involvement in catalysis. Modeling of a DNA-RNA helix together with, structure-based site-directed mutagenesis provides insight into the, mechanism of template DNA binding and RNA primer synthesis.
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<StructureSection load='1zt2' size='340' side='right'caption='[[1zt2]], [[Resolution|resolution]] 3.33&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1zt2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZT2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZT2 FirstGlance]. <br>
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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]] 3.33&#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=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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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=1zt2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zt2 OCA], [https://pdbe.org/1zt2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zt2 RCSB], [https://www.ebi.ac.uk/pdbsum/1zt2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zt2 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PRIS_SACS2 PRIS_SACS2] 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. Possesses a template-independent 3'-terminal nucleotidyl transferase activity.[HAMAP-Rule:MF_00700]<ref>PMID:15561142</ref>
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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/zt/1zt2_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=1zt2 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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Primases are DNA-dependent RNA polymerases that synthesize the oligoribonucleotide primers essential to DNA replication. In archaeal and eukaryotic organisms, the core primase is a heterodimeric enzyme composed of a small and a large subunit. Here we report a crystallographic and biochemical analysis of the core primase from the archaeon Sulfolobus solfataricus. The structure provides the first three-dimensional description of the large subunit and its interaction with the small subunit. The evolutionary conservation of amino acids at the protein-protein interface implies that the observed mode of subunit association is conserved among archaeal and eukaryotic primases. The orientation of the large subunit in the core primase probably excludes its direct involvement in catalysis. Modeling of a DNA-RNA helix together with structure-based site-directed mutagenesis provides insight into the mechanism of template DNA binding and RNA primer synthesis.
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==About this Structure==
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Structure of the heterodimeric core primase.,Lao-Sirieix SH, Nookala RK, Roversi P, Bell SD, Pellegrini L Nat Struct Mol Biol. 2005 Dec;12(12):1137-44. Epub 2005 Nov 6. PMID:16273105<ref>PMID:16273105</ref>
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1ZT2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus] with ZN and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZT2 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structure of the heterodimeric core primase., Lao-Sirieix SH, Nookala RK, Roversi P, Bell SD, Pellegrini L, Nat Struct Mol Biol. 2005 Dec;12(12):1137-44. Epub 2005 Nov 6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16273105 16273105]
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</div>
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[[Category: Protein complex]]
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<div class="pdbe-citations 1zt2" style="background-color:#fffaf0;"></div>
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[[Category: Sulfolobus solfataricus]]
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[[Category: Bell, S.D.]]
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[[Category: Lao-Sirieix, S.H.]]
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[[Category: Nookala, R.K.]]
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[[Category: Pellegrini, L.]]
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[[Category: Roversi, P.]]
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[[Category: SO4]]
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[[Category: ZN]]
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[[Category: heterodimeric complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:38:36 2007''
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==See Also==
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*[[RNA polymerase 3D structures|RNA polymerase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Saccharolobus solfataricus]]
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[[Category: Bell SD]]
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[[Category: Lao-Sirieix SH]]
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[[Category: Nookala RK]]
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[[Category: Pellegrini L]]
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[[Category: Roversi P]]

Current revision

Heterodimeric structure of the core primase.

PDB ID 1zt2

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