This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1a0p

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 22:12, 25 December 2014

SITE-SPECIFIC RECOMBINASE, XERD

Structural highlights

1a0p is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[XERD_ECOLI] Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. Binds cooperatively to specific DNA consensus sequences that are separated from XerC binding sites by a short central region, forming the heterotetrameric XerC-XerD complex that recombines DNA substrates. The complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids at ColE1 xer (or cer) and pSC101 (or psi) sites. In the complex XerD specifically exchanges the bottom DNA strands (By similarity).^[1] ^[2]

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 structure of the site-specific recombinase, XerD, that functions in circular chromosome separation, has been solved at 2.5 A resolution and reveals that the protein comprises two domains. The C-terminal domain contains two conserved sequence motifs that are located in similar positions in the structures of XerD, lambda and HP1 integrases. However, the extreme C-terminal regions of the three proteins, containing the active site tyrosine, are very different. In XerD, the arrangement of active site residues supports a cis cleavage mechanism. Biochemical evidence for DNA bending is encompassed in a model that accommodates extensive biochemical and genetic data, and in which the DNA is wrapped around an alpha-helix in a manner similar to that observed for CAP complexed with DNA.

Crystal structure of the site-specific recombinase, XerD.,Subramanya HS, Arciszewska LK, Baker RA, Bird LE, Sherratt DJ, Wigley DB EMBO J. 1997 Sep 1;16(17):5178-87. PMID:9311978^[3]

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

References

↑ Arciszewska LK, Sherratt DJ. Xer site-specific recombination in vitro. EMBO J. 1995 May 1;14(9):2112-20. PMID:7744017
↑ Cornet F, Hallet B, Sherratt DJ. Xer recombination in Escherichia coli. Site-specific DNA topoisomerase activity of the XerC and XerD recombinases. J Biol Chem. 1997 Aug 29;272(35):21927-31. PMID:9268326
↑ Subramanya HS, Arciszewska LK, Baker RA, Bird LE, Sherratt DJ, Wigley DB. Crystal structure of the site-specific recombinase, XerD. EMBO J. 1997 Sep 1;16(17):5178-87. PMID:9311978 doi:http://dx.doi.org/10.1093/emboj/16.17.5178

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1a0p"

@@ Line 5: / Line 5: @@
 </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=1a0p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a0p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a0p RCSB], [http://www.ebi.ac.uk/pdbsum/1a0p PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/XERD_ECOLI XERD_ECOLI]] Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. Binds cooperatively to specific DNA consensus sequences that are separated from XerC binding sites by a short central region, forming the heterotetrameric XerC-XerD complex that recombines DNA substrates. The complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids at ColE1 xer (or cer) and pSC101 (or psi) sites. In the complex XerD specifically exchanges the bottom DNA strands (By similarity).<ref>PMID:7744017</ref> <ref>PMID:9268326</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1a0p

From Proteopedia

Revision as of 22:12, 25 December 2014

SITE-SPECIFIC RECOMBINASE, XERD

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox