This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1q57

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 07:43, 9 December 2020

The Crystal Structure of the Bifunctional Primase-Helicase of Bacteriophage T7

Structural highlights

1q57 is a 7 chain structure with sequence from Bpt7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1e0j, 1cr0, 1nui, 1e0k, 1cr1, 1cr2, 1cr4
Gene:	4 (BPT7)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PRIM_BPT7] Synthesizes short RNA primers for DNA replication. Unwinds the DNA at the replication forks and generates single-stranded DNA for both leading and lagging strand synthesis. The primase synthesizes short RNA primers on the lagging strand that the polymerase elongates using dNTPs.^[1] ^[2] ^[3]

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

Within minutes after infecting Escherichia coli, bacteriophage T7 synthesizes many copies of its genomic DNA. The lynchpin of the T7 replication system is a bifunctional primase-helicase that unwinds duplex DNA at the replication fork while initiating the synthesis of Okazaki fragments on the lagging strand. We have determined a 3.45 A crystal structure of the T7 primase-helicase that shows an articulated arrangement of the primase and helicase sites. The crystallized primase-helicase is a heptamer with a crown-like shape, reflecting an intimate packing of helicase domains into a ring that is topped with loosely arrayed primase domains. This heptameric isoform can accommodate double-stranded DNA in its central channel, which nicely explains its recently described DNA remodeling activity. The double-jointed structure of the primase-helicase permits a free range of motion for the primase and helicase domains that suggests how the continuous unwinding of DNA at the replication fork can be periodically coupled to Okazaki fragment synthesis.

The crystal structure of the bifunctional primase-helicase of bacteriophage T7.,Toth EA, Li Y, Sawaya MR, Cheng Y, Ellenberger T Mol Cell. 2003 Nov;12(5):1113-23. PMID:14636571^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Kong D, Griffith JD, Richardson CC. Gene 4 helicase of bacteriophage T7 mediates strand transfer through pyrimidine dimers, mismatches, and nonhomologous regions. Proc Natl Acad Sci U S A. 1997 Apr 1;94(7):2987-92. PMID:9096333
↑ Zhang H, Lee SJ, Zhu B, Tran NQ, Tabor S, Richardson CC. Helicase-DNA polymerase interaction is critical to initiate leading-strand DNA synthesis. Proc Natl Acad Sci U S A. 2011 Jun 7;108(23):9372-7. doi:, 10.1073/pnas.1106678108. Epub 2011 May 23. PMID:21606333 doi:http://dx.doi.org/10.1073/pnas.1106678108
↑ Kulczyk AW, Akabayov B, Lee SJ, Bostina M, Berkowitz SA, Richardson CC. An interaction between DNA polymerase and helicase is essential for the high processivity of the bacteriophage T7 replisome. J Biol Chem. 2012 Nov 9;287(46):39050-60. doi: 10.1074/jbc.M112.410647. Epub 2012, Sep 12. PMID:22977246 doi:http://dx.doi.org/10.1074/jbc.M112.410647
↑ Toth EA, Li Y, Sawaya MR, Cheng Y, Ellenberger T. The crystal structure of the bifunctional primase-helicase of bacteriophage T7. Mol Cell. 2003 Nov;12(5):1113-23. PMID:14636571

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1q57"

@@ Line 1: / Line 1: @@
 ==The Crystal Structure of the Bifunctional Primase-Helicase of Bacteriophage T7==
-<StructureSection load='1q57' size='340' side='right' caption='[[1q57]], [[Resolution|resolution]] 3.45&Aring;' scene=''>
+<StructureSection load='1q57' size='340' side='right'caption='[[1q57]], [[Resolution|resolution]] 3.45&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1q57]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpt7 Bpt7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q57 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Q57 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1q57]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpt7 Bpt7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q57 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1Q57 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1e0j|1e0j]], [[1cr0|1cr0]], [[1nui|1nui]], [[1e0k|1e0k]], [[1cr1|1cr1]], [[1cr2|1cr2]], [[1cr4|1cr4]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1e0j|1e0j]], [[1cr0|1cr0]], [[1nui|1nui]], [[1e0k|1e0k]], [[1cr1|1cr1]], [[1cr2|1cr2]], [[1cr4|1cr4]]</div></td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10760 BPT7])</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=1q57 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q57 OCA], [http://pdbe.org/1q57 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1q57 RCSB], [http://www.ebi.ac.uk/pdbsum/1q57 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1q57 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=1q57 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q57 OCA], [http://pdbe.org/1q57 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1q57 RCSB], [http://www.ebi.ac.uk/pdbsum/1q57 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1q57 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 29: / Line 29: @@
 </div>
 <div class="pdbe-citations 1q57" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[RNA polymerase 3D structures|RNA polymerase 3D structures]]
 == References ==
 <references/>
@@ Line 34: / Line 37: @@
 </StructureSection>
 [[Category: Bpt7]]
+[[Category: Large Structures]]
 [[Category: Cheng, Y]]
 [[Category: Ellenberger, T]]

1q57

From Proteopedia

Revision as of 07:43, 9 December 2020

The Crystal Structure of the Bifunctional Primase-Helicase of Bacteriophage T7

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox