6bbm: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
Line 3: Line 3:
<SX load='6bbm' size='340' side='right' viewer='molstar' caption='[[6bbm]], [[Resolution|resolution]] 4.10&Aring;' scene=''>
<SX load='6bbm' size='340' side='right' viewer='molstar' caption='[[6bbm]], [[Resolution|resolution]] 4.10&Aring;' scene=''>
== Structural highlights ==
== 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://proteopedia.org/fgij/fg.htm?mol=6BBM FirstGlance]. <br>
<table><tr><td colspan='2'>[[6bbm]] is a 11 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O111:NM Escherichia coli O111:NM] and [https://en.wikipedia.org/wiki/Escherichia_virus_Lambda Escherichia virus Lambda]. 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 [https://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" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.1&#8491;</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='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='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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6bbm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bbm OCA], [https://pdbe.org/6bbm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bbm RCSB], [https://www.ebi.ac.uk/pdbsum/6bbm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bbm ProSAT]</span></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://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>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/A0A365Q7M1_ECOLX 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] [[http://www.uniprot.org/uniprot/VRPP_LAMBD 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.
[https://www.uniprot.org/uniprot/DNAB_ECOLI DNAB_ECOLI] 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.
<div style="background-color:#fffaf0;">
== 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<ref>PMID:30582519</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6bbm" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Helicase 3D structures|Helicase 3D structures]]
*[[Helicase 3D structures|Helicase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</SX>
</SX>
[[Category: Bacteriophage lambda]]
[[Category: Escherichia coli O111:NM]]
[[Category: DNA helicase]]
[[Category: Escherichia virus Lambda]]
[[Category: Escherichia coli o111:nm]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Catalano, A]]
[[Category: Catalano A]]
[[Category: Chain, B]]
[[Category: Chain B]]
[[Category: Chase, J]]
[[Category: Chase J]]
[[Category: Eng, E T]]
[[Category: Eng ET]]
[[Category: Georges, A des]]
[[Category: Jeruzalmi D]]
[[Category: Jeruzalmi, D]]
[[Category: Molloy K]]
[[Category: Molloy, K]]
[[Category: Noble AJ]]
[[Category: Noble, A J]]
[[Category: Olinares PDB]]
[[Category: Olinares, P D.B]]
[[Category: Pakotiprapha D]]
[[Category: Pakotiprapha, D]]
[[Category: Samuels M]]
[[Category: Samuels, M]]
[[Category: Des Georges A]]
[[Category: Atpase]]
[[Category: Dna replication]]
[[Category: Dna replication initiation]]
[[Category: Helicase]]
[[Category: Helicase loader]]
[[Category: Replication]]

Latest revision as of 17:21, 13 March 2024

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

6bbm, resolution 4.10Å

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=6bbm&oldid=4090586"