1f4k

From Proteopedia

(Difference between revisions)

Revision as of 07:18, 17 March 2021

CRYSTAL STRUCTURE OF THE REPLICATION TERMINATOR PROTEIN/B-SITE DNA COMPLEX

Structural highlights

1f4k is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1bm9
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RTP_BACSU] Plays a role in DNA replication and termination (fork arrest mechanism). Two dimers of rtp bind to the two inverted repeat regions (IRI and IRII) present in the termination site. The binding of each dimer is centered on an 8 bp direct repeat.

Publication Abstract from PubMed

The coordinated termination of DNA replication is an important step in the life cycle of bacteria with circular chromosomes, but has only been defined at a molecular level in two systems to date. Here we report the structure of an engineered replication terminator protein (RTP) of Bacillus subtilis in complex with a 21 base pair DNA by X-ray crystallography at 2.5 A resolution. We also use NMR spectroscopic titration techniques. This work reveals a novel DNA interaction involving a dimeric 'winged helix' domain protein that differs from predictions. While the two recognition helices of RTP are in close contact with the B-form DNA major grooves, the 'wings' and N-termini of RTP do not form intimate contacts with the DNA. This structure provides insight into the molecular basis of polar replication fork arrest based on a model of cooperative binding and differential binding affinities of RTP to the two adjacent binding sites in the complete terminator.

Structure of the RTP-DNA complex and the mechanism of polar replication fork arrest.,Wilce JA, Vivian JP, Hastings AF, Otting G, Folmer RH, Duggin IG, Wake RG, Wilce MC Nat Struct Biol. 2001 Mar;8(3):206-10. PMID:11224562^[1]

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

References

↑ Wilce JA, Vivian JP, Hastings AF, Otting G, Folmer RH, Duggin IG, Wake RG, Wilce MC. Structure of the RTP-DNA complex and the mechanism of polar replication fork arrest. Nat Struct Biol. 2001 Mar;8(3):206-10. PMID:11224562 doi:10.1038/84934

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/1f4k"

@@ Line 3: / Line 3: @@
 <StructureSection load='1f4k' size='340' side='right'caption='[[1f4k]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1f4k]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F4K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F4K FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1f4k]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F4K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F4K FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bm9|1bm9]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1bm9|1bm9]]</div></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=1f4k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f4k OCA], [http://pdbe.org/1f4k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1f4k RCSB], [http://www.ebi.ac.uk/pdbsum/1f4k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1f4k ProSAT]</span></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=1f4k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f4k OCA], [https://pdbe.org/1f4k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f4k RCSB], [https://www.ebi.ac.uk/pdbsum/1f4k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f4k ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/RTP_BACSU RTP_BACSU]] Plays a role in DNA replication and termination (fork arrest mechanism). Two dimers of rtp bind to the two inverted repeat regions (IRI and IRII) present in the termination site. The binding of each dimer is centered on an 8 bp direct repeat.
+[[https://www.uniprot.org/uniprot/RTP_BACSU RTP_BACSU]] Plays a role in DNA replication and termination (fork arrest mechanism). Two dimers of rtp bind to the two inverted repeat regions (IRI and IRII) present in the termination site. The binding of each dimer is centered on an 8 bp direct repeat.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 20: / Line 20: @@
 ==See Also==
-*[[Bacterial Replication Termination|Bacterial Replication Termination]]
 *[[Replication Termination Protein|Replication Termination Protein]]
 *[[Tomato aspermy virus protein 2b Suppression of RNA Silencing|Tomato aspermy virus protein 2b Suppression of RNA Silencing]]
-*[[User:Chloe Paul/Replication Terminator Protein|User:Chloe Paul/Replication Terminator Protein]]
-*[[User:Wayne Decatur/Tomato aspermy virus protein 2b Suppression of RNA Silencing|User:Wayne Decatur/Tomato aspermy virus protein 2b Suppression of RNA Silencing]]
 == References ==
 <references/>

1f4k

From Proteopedia

Revision as of 07:18, 17 March 2021

CRYSTAL STRUCTURE OF THE REPLICATION TERMINATOR PROTEIN/B-SITE DNA COMPLEX

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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