4m4w

From Proteopedia

(Difference between revisions)

Revision as of 13:19, 25 December 2014

Mechanistic implications for the bacterial primosome assembly of the structure of a helicase-helicase loader complex

Structural highlights

4m4w is a 15 chain structure with sequence from Bacillus subtilis subsp. subtilis str. 168 and Geobacillus stearothermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Gene:	dnaB (Geobacillus stearothermophilus), dnaG (Geobacillus stearothermophilus), BSU28980, dnaI, ytxA (Bacillus subtilis subsp. subtilis str. 168)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[DNAI_BACSU] Probably involved in DNA replication. [PRIM_GEOSE] DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments on both template strands at replication forks during chromosomal DNA synthesis.

Publication Abstract from PubMed

During the assembly of the bacterial loader-dependent primosome, helicase loader proteins bind to the hexameric helicase ring, deliver it onto the oriC DNA and then dissociate from the complex. Here, to provide a better understanding of this key process, we report the crystal structure of the ~570-kDa prepriming complex between the Bacillus subtilis loader protein and the Bacillus stearothermophilus helicase, as well as the helicase-binding domain of primase with a molar ratio of 6:6:3 at 7.5 A resolution. The overall architecture of the complex exhibits a three-layered ring conformation. Moreover, the structure combined with the proposed model suggests that the shift from the 'open-ring' to the 'open-spiral' and then the 'closed-spiral' state of the helicase ring due to the binding of single-stranded DNA may be the cause of the loader release.

Structure of a helicase-helicase loader complex reveals insights into the mechanism of bacterial primosome assembly.,Liu B, Eliason WK, Steitz TA Nat Commun. 2013;4:2495. doi: 10.1038/ncomms3495. PMID:24048025^[1]

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

References

↑ Liu B, Eliason WK, Steitz TA. Structure of a helicase-helicase loader complex reveals insights into the mechanism of bacterial primosome assembly. Nat Commun. 2013;4:2495. doi: 10.1038/ncomms3495. PMID:24048025 doi:10.1038/ncomms3495

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/4m4w"

@@ Line 7: / Line 7: @@
 <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=4m4w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m4w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4m4w RCSB], [http://www.ebi.ac.uk/pdbsum/4m4w PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/DNAI_BACSU DNAI_BACSU]] Probably involved in DNA replication. [[http://www.uniprot.org/uniprot/PRIM_GEOSE PRIM_GEOSE]] DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments on both template strands at replication forks during chromosomal DNA synthesis.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

4m4w

From Proteopedia

Revision as of 13:19, 25 December 2014

Mechanistic implications for the bacterial primosome assembly of the structure of a helicase-helicase loader complex

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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