1ecr

From Proteopedia

(Difference between revisions)

@@ Line 1: / Line 1: @@
 ==ESCHERICHIA COLI REPLICATION TERMINATOR PROTEIN (TUS) COMPLEXED WITH DNA==
-<StructureSection load='1ecr' size='340' side='right' caption='[[1ecr]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
+<StructureSection load='1ecr' size='340' side='right'caption='[[1ecr]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1ecr]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_(strain_b) Escherichia coli (strain b)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ECR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ECR FirstGlance]. <br>
@@ Line 27: / Line 27: @@
 </div>
 <div class="pdbe-citations 1ecr" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Replication Termination Protein|Replication Termination Protein]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Kamada, K]]
 [[Category: Morikawa, K]]

Revision as of 08:45, 23 October 2019

ESCHERICHIA COLI REPLICATION TERMINATOR PROTEIN (TUS) COMPLEXED WITH DNA

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PDB ID 1ecr

Show:Asymmetric Unit Biological Assembly

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Structural highlights

1ecr is a 3 chain structure with sequence from Escherichia coli (strain b). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[TUS_ECOLI] Trans-acting protein required for termination of DNA replication. Binds to DNA replication terminator sequences (terA to terF) to prevent the passage of replication forks. The termination efficiency will be affected by the affinity of this protein for the terminator sequence.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The crystal structure of the Escherichia coli replication-terminator protein (Tus) bound to terminus-site (Ter) DNA has been determined at 2.7 A resolution. The Tus protein folds into a previously undescribed architecture divided into two domains by a central basic cleft. This cleft accommodates locally deformed B-form Ter DNA and makes extensive contacts with the major groove, mainly through two interdomain beta-strands. The unusual structural features of this complex may explain how the replication fork is halted in only one direction.

Structure of a replication-terminator protein complexed with DNA.,Kamada K, Horiuchi T, Ohsumi K, Shimamoto N, Morikawa K Nature. 1996 Oct 17;383(6601):598-603. PMID:8857533^[1]

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

References

↑ Kamada K, Horiuchi T, Ohsumi K, Shimamoto N, Morikawa K. Structure of a replication-terminator protein complexed with DNA. Nature. 1996 Oct 17;383(6601):598-603. PMID:8857533 doi:http://dx.doi.org/10.1038/383598a0

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

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1ecr

From Proteopedia

Revision as of 08:45, 23 October 2019

ESCHERICHIA COLI REPLICATION TERMINATOR PROTEIN (TUS) COMPLEXED WITH DNA

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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