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| | <StructureSection load='5guj' size='340' side='right'caption='[[5guj]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='5guj' size='340' side='right'caption='[[5guj]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5guj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacsu Bacsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GUJ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5GUJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5guj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GUJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GUJ FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5gum|5gum]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dnaG, dnaE, BSU25210 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</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=5guj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5guj OCA], [https://pdbe.org/5guj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5guj RCSB], [https://www.ebi.ac.uk/pdbsum/5guj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5guj ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5guj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5guj OCA], [http://pdbe.org/5guj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5guj RCSB], [http://www.ebi.ac.uk/pdbsum/5guj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5guj ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DNAG_BACSU DNAG_BACSU]] RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.[HAMAP-Rule:MF_00974] | + | [https://www.uniprot.org/uniprot/DNAG_BACSU DNAG_BACSU] RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.[HAMAP-Rule:MF_00974] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacsu]] | + | [[Category: Bacillus subtilis subsp. subtilis str. 168]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Liu, Z]] | + | [[Category: Liu Z]] |
| - | [[Category: Wang, G]] | + | [[Category: Wang G]] |
| - | [[Category: Zhou, Y]] | + | [[Category: Zhou Y]] |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
DNAG_BACSU RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.[HAMAP-Rule:MF_00974]
Publication Abstract from PubMed
Bacterial primase initiates the repeated synthesis of short RNA primers that are extended by DNA polymerase to synthesize Okazaki fragments on the lagging strand at replication forks. It remains unclear how the enzyme recognizes specific initiation sites. In this study, the DnaG primase from Bacillus subtilis (BsuDnaG) was characterized and the crystal structure of the RNA polymerase domain (RPD) was determined. Structural comparisons revealed that the tethered zinc binding domain plays an important role in the interactions between primase and specific template sequence. Structural and biochemical data defined the ssDNA template binding surface as an L shape, and a model for the template ssDNA binding to primase is proposed. The flexibility of the DnaG primases from B. subtilis and G. stearothermophilus were compared, and the results implied that the intrinsic flexibility of the primase may facilitate the interactions between primase and various partners in the replisome. These results shed light on the mechanism by which DnaG recognizes the specific initiation site.
Structural Insight into the Specific DNA Template Binding to DnaG primase in Bacteria.,Zhou Y, Luo H, Liu Z, Yang M, Pang X, Sun F, Wang G Sci Rep. 2017 Apr 6;7(1):659. doi: 10.1038/s41598-017-00767-8. PMID:28386108[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zhou Y, Luo H, Liu Z, Yang M, Pang X, Sun F, Wang G. Structural Insight into the Specific DNA Template Binding to DnaG primase in Bacteria. Sci Rep. 2017 Apr 6;7(1):659. doi: 10.1038/s41598-017-00767-8. PMID:28386108 doi:http://dx.doi.org/10.1038/s41598-017-00767-8
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