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6bbm

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Revision as of 23:18, 10 April 2020

Mechanisms of Opening and Closing of the Bacterial Replicative Helicase: The DnaB Helicase and Lambda P Helicase Loader Complex

6bbm, resolution 4.10Å

Structural highlights

6bbm is a 11 chain structure with sequence from Bacteriophage lambda and Escherichia coli o111:nm. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	DQW49_15020 (Escherichia coli O111:NM)
Activity:	DNA helicase, with EC number 3.6.4.12
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[A0A365Q7M1_ECOLX] Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity and contains distinct active sites for ATP binding, DNA binding, and interaction with DnaC protein, primase, and other prepriming proteins.[RuleBase:RU362085] [VRPP_LAMBD] Replication protein P is necessary for the bidirectional replication of lambda DNA. It interacts with the ori (origin of replication) region of the genome during the initiation of replication.

Publication Abstract from PubMed

Assembly of bacterial ring-shaped hexameric replicative helicases on single-stranded (ss) DNA requires specialized loading factors. However, mechanisms implemented by these factors during opening and closing of the helicase, which enable and restrict access to an internal chamber, are not known. Here, we investigate these mechanisms in the Escherichia coli DnaB helicase*bacteriophage lambda helicase loader (lambdaP) complex. We show that five copies of lambdaP bind at DnaB subunit interfaces and reconfigure the helicase into an open spiral conformation that is intermediate to previously observed closed ring and closed spiral forms; reconfiguration also produces openings large enough to admit ssDNA into the inner chamber. The helicase is also observed in a restrained inactive configuration that poises it to close on activating signal, and transition to the translocation state. Our findings provide insights into helicase opening, delivery to the origin and ssDNA entry, and closing in preparation for translocation.

Mechanisms of opening and closing of the bacterial replicative helicase.,Chase J, Catalano A, Noble AJ, Eng ET, Olinares PD, Molloy K, Pakotiprapha D, Samuels M, Chait B, des Georges A, Jeruzalmi D Elife. 2018 Dec 24;7. pii: 41140. doi: 10.7554/eLife.41140. PMID:30582519^[1]

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

References

↑ Chase J, Catalano A, Noble AJ, Eng ET, Olinares PD, Molloy K, Pakotiprapha D, Samuels M, Chait B, des Georges A, Jeruzalmi D. Mechanisms of opening and closing of the bacterial replicative helicase. Elife. 2018 Dec 24;7. pii: 41140. doi: 10.7554/eLife.41140. PMID:30582519 doi:http://dx.doi.org/10.7554/eLife.41140

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6bbm"

@@ Line 3: / Line 3: @@
 <SX load='6bbm' size='340' side='right' viewer='molstar' caption='[[6bbm]], [[Resolution|resolution]] 4.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6bbm]] is a 11 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacteriophage_lambda Bacteriophage lambda] and [http://en.wikipedia.org/wiki/Escherichia_coli_o111:nm Escherichia coli o111:nm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BBM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BBM FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6bbm]] is a 11 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacteriophage_lambda Bacteriophage lambda] and [http://en.wikipedia.org/wiki/Escherichia_coli_o111:nm Escherichia coli o111:nm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BBM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6BBM FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DQW49_15020 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=373045 Escherichia coli O111:NM])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_helicase DNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.12 3.6.4.12] </span></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=6bbm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bbm OCA], [http://pdbe.org/6bbm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bbm RCSB], [http://www.ebi.ac.uk/pdbsum/6bbm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bbm 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=6bbm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bbm OCA], [http://pdbe.org/6bbm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bbm RCSB], [http://www.ebi.ac.uk/pdbsum/6bbm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bbm ProSAT]</span></td></tr>
 </table>
 == Function ==

6bbm

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Revision as of 23:18, 10 April 2020

Mechanisms of Opening and Closing of the Bacterial Replicative Helicase: The DnaB Helicase and Lambda P Helicase Loader Complex

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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