4e2k
From Proteopedia
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| - | + | ==The structure of the S. aureus DnaG RNA Polymerase Domain== | |
| - | + | <StructureSection load='4e2k' size='340' side='right' caption='[[4e2k]], [[Resolution|resolution]] 2.15Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4e2k]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E2K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E2K FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BEN:BENZAMIDINE'>BEN</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dnaG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus])</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4e2k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e2k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e2k RCSB], [http://www.ebi.ac.uk/pdbsum/4e2k PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Primases are DNA-dependent RNA polymerases found in all cellular organisms. In bacteria, primer synthesis is carried out by DnaG, an essential enzyme that serves as a key component of DNA replication initiation, progression, and restart. How DnaG associates with nucleotide substrates and how certain naturally prevalent nucleotide analogs impair DnaG function are unknown. We have examined one of the earliest stages in primer synthesis and its control by solving crystal structures of the S. aureus DnaG catalytic core bound to metal ion cofactors and either individual nucleoside triphosphates or the nucleotidyl alarmones, pppGpp and ppGpp. These structures, together with both biochemical analyses and comparative studies of enzymes that use the same catalytic fold as DnaG, pinpoint the predominant nucleotide-binding site of DnaG and explain how the induction of the stringent response in bacteria interferes with primer synthesis. | ||
| - | + | Binding Mechanism of MetalNTP Substrates and Stringent-Response Alarmones to Bacterial DnaG-Type Primases.,Rymer RU, Solorio FA, Tehranchi AK, Chu C, Corn JE, Keck JL, Wang JD, Berger JM Structure. 2012 Jul 10. PMID:22795082<ref>PMID:22795082</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | == | + | ==See Also== |
| - | + | *[[RNA polymerase|RNA polymerase]] | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Staphylococcus aureus]] | [[Category: Staphylococcus aureus]] | ||
| - | [[Category: Berger, J M | + | [[Category: Berger, J M]] |
| - | [[Category: Clement, C | + | [[Category: Clement, C]] |
| - | [[Category: Corn, J E | + | [[Category: Corn, J E]] |
| - | [[Category: Rymer, R U | + | [[Category: Rymer, R U]] |
| - | [[Category: Solorio, F A | + | [[Category: Solorio, F A]] |
| - | [[Category: Wang, J D | + | [[Category: Wang, J D]] |
[[Category: Apo protein]] | [[Category: Apo protein]] | ||
[[Category: Bacterial]] | [[Category: Bacterial]] | ||
[[Category: Catalytic domain]] | [[Category: Catalytic domain]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 11:40, 21 December 2014
The structure of the S. aureus DnaG RNA Polymerase Domain
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