2c5r: Difference between revisions

Latest revision as of 10:24, 6 September 2023

The structure of phage phi29 replication organizer protein p16.7 in complex with double stranded DNA

Structural highlights

2c5r is a 8 chain structure with sequence from Bacillus virus phi29. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.9Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GP167_BPPH2 Binds to the long stretches of ssDNA of the viral DNA replication intermediates created during the protein-primed mechanism of replication of the viral genome and attaches the viral DNA to the membrane of the infected cells (PubMed:11741949) (PubMed:11169113). Required for the redistribution of replicating viral DNA from the initial replication site to membrane-associated sites surrounding the nucleoid (PubMed:10921898). Required for the second pull step of DNA ejection (PubMed:17526715).^[1] ^[2] ^[3] ^[4]

Publication Abstract from PubMed

Prokaryotic DNA replication is compartmentalized at the cellular membrane. Functional and biochemical studies showed that the Bacillus subtilis phage 29-encoded membrane protein p16.7 is directly involved in the organization of membrane-associated viral DNA replication. The structure of the functional domain of p16.7 in complex with DNA, presented here, reveals the multimerization mode of the protein and provides insights in the organization of the phage genome at the membrane of the infected cell.

Structural basis for membrane anchorage of viral phi29 DNA during replication.,Albert A, Munoz-Espin D, Jimenez M, Asensio JL, Hermoso JA, Salas M, Meijer WJ J Biol Chem. 2005 Dec 30;280(52):42486-8. Epub 2005 Nov 7. PMID:16275651^[5]

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

References

↑ Meijer WJ, Lewis PJ, Errington J, Salas M. Dynamic relocalization of phage phi 29 DNA during replication and the role of the viral protein p16.7. EMBO J. 2000 Aug 1;19(15):4182-90. PMID:10921898 doi:10.1093/emboj/19.15.4182
↑ Meijer WJ, Serna-Rico A, Salas M. Characterization of the bacteriophage phi29-encoded protein p16.7: a membrane protein involved in phage DNA replication. Mol Microbiol. 2001 Feb;39(3):731-46. PMID:11169113 doi:10.1046/j.1365-2958.2001.02260.x
↑ Serna-Rico A, Salas M, Meijer WJ. The Bacillus subtilis phage phi 29 protein p16.7, involved in phi 29 DNA replication, is a membrane-localized single-stranded DNA-binding protein. J Biol Chem. 2002 Feb 22;277(8):6733-42. PMID:11741949 doi:10.1074/jbc.M109312200
↑ Alcorlo M, González-Huici V, Hermoso JM, Meijer WJ, Salas M. The phage phi29 membrane protein p16.7, involved in DNA replication, is required for efficient ejection of the viral genome. J Bacteriol. 2007 Aug;189(15):5542-9. PMID:17526715 doi:10.1128/JB.00402-07
↑ Albert A, Munoz-Espin D, Jimenez M, Asensio JL, Hermoso JA, Salas M, Meijer WJ. Structural basis for membrane anchorage of viral phi29 DNA during replication. J Biol Chem. 2005 Dec 30;280(52):42486-8. Epub 2005 Nov 7. PMID:16275651 doi:C500429200

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OCA

[1] Meijer WJ, Lewis PJ, Errington J, Salas M. Dynamic relocalization of phage phi 29 DNA during replication and the role of the viral protein p16.7. EMBO J. 2000 Aug 1;19(15):4182-90. PMID:10921898 doi:10.1093/emboj/19.15.4182

[2] Meijer WJ, Serna-Rico A, Salas M. Characterization of the bacteriophage phi29-encoded protein p16.7: a membrane protein involved in phage DNA replication. Mol Microbiol. 2001 Feb;39(3):731-46. PMID:11169113 doi:10.1046/j.1365-2958.2001.02260.x

[3] Serna-Rico A, Salas M, Meijer WJ. The Bacillus subtilis phage phi 29 protein p16.7, involved in phi 29 DNA replication, is a membrane-localized single-stranded DNA-binding protein. J Biol Chem. 2002 Feb 22;277(8):6733-42. PMID:11741949 doi:10.1074/jbc.M109312200

[4] Alcorlo M, González-Huici V, Hermoso JM, Meijer WJ, Salas M. The phage phi29 membrane protein p16.7, involved in DNA replication, is required for efficient ejection of the viral genome. J Bacteriol. 2007 Aug;189(15):5542-9. PMID:17526715 doi:10.1128/JB.00402-07

[5] Albert A, Munoz-Espin D, Jimenez M, Asensio JL, Hermoso JA, Salas M, Meijer WJ. Structural basis for membrane anchorage of viral phi29 DNA during replication. J Biol Chem. 2005 Dec 30;280(52):42486-8. Epub 2005 Nov 7. PMID:16275651 doi:C500429200

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[2]

[3]

[4]

[5]

@@ Line 3: / Line 3: @@
 <StructureSection load='2c5r' size='340' side='right'caption='[[2c5r]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2c5r]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Bpph2 Bpph2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C5R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C5R FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2c5r]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_virus_phi29 Bacillus virus phi29]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C5R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C5R 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;'>[[1zae|1zae]], [[2bnk|2bnk]]</div></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]] 2.9&#8491;</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=2c5r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c5r OCA], [https://pdbe.org/2c5r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c5r RCSB], [https://www.ebi.ac.uk/pdbsum/2c5r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c5r ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/GP167_BPPH2 GP167_BPPH2] Binds to the long stretches of ssDNA of the viral DNA replication intermediates created during the protein-primed mechanism of replication of the viral genome and attaches the viral DNA to the membrane of the infected cells (PubMed:11741949) (PubMed:11169113). Required for the redistribution of replicating viral DNA from the initial replication site to membrane-associated sites surrounding the nucleoid (PubMed:10921898). Required for the second pull step of DNA ejection (PubMed:17526715).<ref>PMID:10921898</ref> <ref>PMID:11169113</ref> <ref>PMID:11741949</ref> <ref>PMID:17526715</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 20: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Bpph2]]
+[[Category: Bacillus virus phi29]]
 [[Category: Large Structures]]
-[[Category: Albert, A]]
+[[Category: Albert A]]
-[[Category: Asensio, J L]]
+[[Category: Asensio JL]]
-[[Category: Hermoso, J A]]
+[[Category: Hermoso JA]]
-[[Category: Jimenez, M]]
+[[Category: Jimenez M]]
-[[Category: Meijer, W J.J]]
+[[Category: Meijer WJJ]]
-[[Category: Munoz-Espin, D]]
+[[Category: Munoz-Espin D]]
-[[Category: Salas, M]]
+[[Category: Salas M]]
-[[Category: Dna-binding protein]]
-[[Category: Dna-binding protein-dna complex]]

2c5r: Difference between revisions

Latest revision as of 10:24, 6 September 2023

The structure of phage phi29 replication organizer protein p16.7 in complex with double stranded DNA

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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