|
|
| Line 1: |
Line 1: |
| | | | |
| | ==Solution structure of the helicase-binding domain of Escherichia coli primase== | | ==Solution structure of the helicase-binding domain of Escherichia coli primase== |
| - | <StructureSection load='2haj' size='340' side='right'caption='[[2haj]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2haj' size='340' side='right'caption='[[2haj]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2haj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HAJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HAJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2haj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HAJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HAJ FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1t3w|1t3w]]</div></td></tr> | + | </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=2haj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2haj OCA], [https://pdbe.org/2haj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2haj RCSB], [https://www.ebi.ac.uk/pdbsum/2haj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2haj ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dnaG ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=2haj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2haj OCA], [https://pdbe.org/2haj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2haj RCSB], [https://www.ebi.ac.uk/pdbsum/2haj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2haj ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/PRIM_ECOLI PRIM_ECOLI]] DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments on both template strands at replication forks during chromosomal DNA synthesis.
| + | [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> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 36: |
Line 34: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dixon, N E]] | + | [[Category: Dixon NE]] |
| - | [[Category: Loscha, K V]] | + | [[Category: Loscha KV]] |
| - | [[Category: Otting, G]] | + | [[Category: Otting G]] |
| - | [[Category: Su, X C]] | + | [[Category: Su XC]] |
| - | [[Category: Dna polymerase]]
| + | |
| - | [[Category: Helicase]]
| + | |
| - | [[Category: Helix]]
| + | |
| - | [[Category: Primase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
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][1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
DnaG is the primase that lays down RNA primers on single-stranded DNA during bacterial DNA replication. The solution structure of the DnaB-helicase-binding C-terminal domain of Escherichia coli DnaG was determined by NMR spectroscopy at near-neutral pH. The structure is a rare fold that, besides occurring in DnaG C-terminal domains, has been described only for the N-terminal domain of DnaB. The C-terminal helix hairpin present in the DnaG C-terminal domain, however, is either less stable or absent in DnaB, as evidenced by high mobility of the C-terminal 35 residues in a construct comprising residues 1-171. The present structure identifies the previous crystal structure of the E. coli DnaG C-terminal domain as a domain-swapped dimer. It is also significantly different from the NMR structure reported for the corresponding domain of DnaG from the thermophile Bacillus stearothermophilus. NMR experiments showed that the DnaG C-terminal domain does not bind to residues 1-171 of the E. coli DnaB helicase with significant affinity.
Monomeric solution structure of the helicase-binding domain of Escherichia coli DnaG primase.,Su XC, Schaeffer PM, Loscha KV, Gan PH, Dixon NE, Otting G FEBS J. 2006 Nov;273(21):4997-5009. Epub 2006 Sep 28. PMID:17010164[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Stamford NP, Lilley PE, Dixon NE. Enriched sources of Escherichia coli replication proteins. The dnaG primase is a zinc metalloprotein. Biochim Biophys Acta. 1992 Aug 17;1132(1):17-25. PMID:1511009
- ↑ Rowen L, Kornberg A. Primase, the dnaG protein of Escherichia coli. An enzyme which starts DNA chains. J Biol Chem. 1978 Feb 10;253(3):758-64. PMID:340457
- ↑ Su XC, Schaeffer PM, Loscha KV, Gan PH, Dixon NE, Otting G. Monomeric solution structure of the helicase-binding domain of Escherichia coli DnaG primase. FEBS J. 2006 Nov;273(21):4997-5009. Epub 2006 Sep 28. PMID:17010164 doi:http://dx.doi.org/10.1111/j.1742-4658.2006.05495.x
|
