6qem

From Proteopedia

(Difference between revisions)

Revision as of 07:06, 17 April 2019

E. coli DnaBC complex bound to ssDNA

Structural highlights

6qem is a 13 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Gene:	dnaB, groP, grpA, b4052, JW4012 ("Bacillus coli" Migula 1895), dnaC, dnaD, b4361, JW4325 ("Bacillus coli" Migula 1895)
Activity:	DNA helicase, with EC number 3.6.4.12
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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. [DNAC_ECOLI] This protein is required for chromosomal replication. It forms, in concert with DnaB protein and other prepriming proteins DnaT, N, N', N a prepriming protein complex on the specific site of the template DNA recognized by protein N'.

Publication Abstract from PubMed

In cells, dedicated AAA+ ATPases deposit hexameric, ring-shaped helicases onto DNA to initiate chromosomal replication. To better understand the mechanisms by which helicase loading can occur, we used cryo-EM to determine sub-4-A-resolution structures of the E. coli DnaBDnaC helicaseloader complex with nucleotide in pre- and post-DNA engagement states. In the absence of DNA, six DnaC protomers latch onto and crack open a DnaB hexamer using an extended N-terminal domain, stabilizing this conformation through nucleotide-dependent ATPase interactions. Upon binding DNA, DnaC hydrolyzes ATP, allowing DnaB to isomerize into a topologically closed, pre-translocation state competent to bind primase. Our data show how DnaC opens the DnaB ring and represses the helicase prior to DNA binding and how DnaC ATPase activity is reciprocally regulated by DnaB and DNA. Comparative analyses reveal how the helicase loading mechanism of DnaC parallels and diverges from homologous AAA+ systems involved in DNA replication and transposition.

Physical Basis for the Loading of a Bacterial Replicative Helicase onto DNA.,Arias-Palomo E, Puri N, O'Shea Murray VL, Yan Q, Berger JM Mol Cell. 2019 Feb 16. pii: S1097-2765(19)30043-7. doi:, 10.1016/j.molcel.2019.01.023. PMID:30797687^[1]

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

References

↑ Arias-Palomo E, Puri N, O'Shea Murray VL, Yan Q, Berger JM. Physical Basis for the Loading of a Bacterial Replicative Helicase onto DNA. Mol Cell. 2019 Feb 16. pii: S1097-2765(19)30043-7. doi:, 10.1016/j.molcel.2019.01.023. PMID:30797687 doi:http://dx.doi.org/10.1016/j.molcel.2019.01.023

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
 ==E. coli DnaBC complex bound to ssDNA==
-<StructureSection load='6qem' size='340' side='right'  caption='[[6qem]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
+<StructureSection load='6qem' size='340' side='right'caption='[[6qem]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6qem]] is a 13 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QEM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QEM FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6qem]] is a 13 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QEM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QEM FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=08T:[[[(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-BIS(OXIDANYL)OXOLAN-2-YL]METHOXY-OXIDANYL-PHOSPHORYL]OXY-OXIDANYL-PHOSPHORYL]OXY-TRIS(FLUORANYL)BERYLLIUM'>08T</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dnaB, groP, grpA, b4052, JW4012 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895]), dnaC, dnaD, b4361, JW4325 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=6qem FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qem OCA], [http://pdbe.org/6qem PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qem RCSB], [http://www.ebi.ac.uk/pdbsum/6qem PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qem ProSAT]</span></td></tr>
@@ Line 23: / Line 24: @@
 __TOC__
 </StructureSection>
+[[Category: Bacillus coli migula 1895]]
 [[Category: DNA helicase]]
+[[Category: Large Structures]]
 [[Category: Arias-Palomo, E]]
 [[Category: Berger, J M]]

6qem

From Proteopedia

Revision as of 07:06, 17 April 2019

E. coli DnaBC complex bound to ssDNA

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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