1a0p

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(New page: 200px<br /><applet load="1a0p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a0p, resolution 2.5&Aring;" /> '''SITE-SPECIFIC RECOMBI...)
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[[Image:1a0p.jpg|left|200px]]<br /><applet load="1a0p" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1a0p, resolution 2.5&Aring;" />
caption="1a0p, resolution 2.5&Aring;" />
'''SITE-SPECIFIC RECOMBINASE, XERD'''<br />
'''SITE-SPECIFIC RECOMBINASE, XERD'''<br />
==Overview==
==Overview==
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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.
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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.
==About this Structure==
==About this Structure==
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1A0P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A0P OCA].
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1A0P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A0P OCA].
==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Arciszewska, L.K.]]
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[[Category: Arciszewska, L K.]]
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[[Category: Baker, R.A.]]
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[[Category: Baker, R A.]]
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[[Category: Bird, L.E.]]
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[[Category: Bird, L E.]]
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[[Category: Sherratt, D.J.]]
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[[Category: Sherratt, D J.]]
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[[Category: Subramanya, H.S.]]
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[[Category: Subramanya, H S.]]
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[[Category: Wigley, D.B.]]
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[[Category: Wigley, D B.]]
[[Category: dna binding]]
[[Category: dna binding]]
[[Category: dna recombination]]
[[Category: dna recombination]]
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[[Category: xerd]]
[[Category: xerd]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:32:14 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:39:37 2008''

Revision as of 09:39, 21 February 2008


1a0p, resolution 2.5Å

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SITE-SPECIFIC RECOMBINASE, XERD

Overview

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.

About this Structure

1A0P is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

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

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