1eqn

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(New page: 200px<br /><applet load="1eqn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eqn, resolution 2.9&Aring;" /> '''E.COLI PRIMASE CATALY...)
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[[Image:1eqn.gif|left|200px]]<br /><applet load="1eqn" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1eqn, resolution 2.9&Aring;" />
 
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'''E.COLI PRIMASE CATALYTIC CORE'''<br />
 
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==Overview==
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==E.COLI PRIMASE CATALYTIC CORE==
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Primases synthesize short RNA strands on single-stranded DNA templates, thereby generating the hybrid duplexes required for the initiation of, synthesis by DNA polymerases. We present the crystal structure of the, catalytic unit of a primase enzyme, that of a approximately 320 residue, fragment of Escherichia coli primase, determined at 2.9 A resolution., Central to the catalytic unit is a TOPRIM domain that is strikingly, similar in its structure to that of corresponding domains in DNA, topoisomerases, but is unrelated to the catalytic centers of other DNA or, RNA polymerases. The catalytic domain of primase is crescent-shaped, and, the concave face of the crescent is predicted to accommodate about 10, base-pairs of RNA-DNA duplex in a loose interaction, thereby limiting, processivity.
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<StructureSection load='1eqn' size='340' side='right'caption='[[1eqn]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1eqn]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EQN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EQN 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]] 2.9&#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=MSE:SELENOMETHIONINE'>MSE</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=1eqn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eqn OCA], [https://pdbe.org/1eqn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eqn RCSB], [https://www.ebi.ac.uk/pdbsum/1eqn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eqn ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DNAG_ECOLI DNAG_ECOLI] RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.[HAMAP-Rule:MF_00974]<ref>PMID:1511009</ref> <ref>PMID:340457</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/eq/1eqn_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=1eqn 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 synthesize short RNA strands on single-stranded DNA templates, thereby generating the hybrid duplexes required for the initiation of synthesis by DNA polymerases. We present the crystal structure of the catalytic unit of a primase enzyme, that of a approximately 320 residue fragment of Escherichia coli primase, determined at 2.9 A resolution. Central to the catalytic unit is a TOPRIM domain that is strikingly similar in its structure to that of corresponding domains in DNA topoisomerases, but is unrelated to the catalytic centers of other DNA or RNA polymerases. The catalytic domain of primase is crescent-shaped, and the concave face of the crescent is predicted to accommodate about 10 base-pairs of RNA-DNA duplex in a loose interaction, thereby limiting processivity.
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==About this Structure==
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A TOPRIM domain in the crystal structure of the catalytic core of Escherichia coli primase confirms a structural link to DNA topoisomerases.,Podobnik M, McInerney P, O'Donnell M, Kuriyan J J Mol Biol. 2000 Jul 7;300(2):353-62. PMID:10873470<ref>PMID:10873470</ref>
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1EQN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EQN 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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A TOPRIM domain in the crystal structure of the catalytic core of Escherichia coli primase confirms a structural link to DNA topoisomerases., Podobnik M, McInerney P, O'Donnell M, Kuriyan J, J Mol Biol. 2000 Jul 7;300(2):353-62. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10873470 10873470]
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</div>
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[[Category: Escherichia coli]]
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<div class="pdbe-citations 1eqn" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Donnell, M.O.]]
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[[Category: Kuriyan, J.]]
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[[Category: McInerney, P.]]
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[[Category: Podobnik, M.]]
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[[Category: rossmann fold]]
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[[Category: toprim domain]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:14:02 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: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: Kuriyan J]]
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[[Category: McInerney P]]
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[[Category: O'Donnell M]]
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[[Category: Podobnik M]]

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E.COLI PRIMASE CATALYTIC CORE

PDB ID 1eqn

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