1jko

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(New page: 200px<br /><applet load="1jko" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jko, resolution 2.24&Aring;" /> '''Testing the Water-Me...)
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[[Image:1jko.gif|left|200px]]<br /><applet load="1jko" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1jko.gif|left|200px]]<br /><applet load="1jko" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1jko, resolution 2.24&Aring;" />
caption="1jko, resolution 2.24&Aring;" />
'''Testing the Water-Mediated HIN Recombinase DNA Recognition by Systematic Mutations'''<br />
'''Testing the Water-Mediated HIN Recombinase DNA Recognition by Systematic Mutations'''<br />
==Overview==
==Overview==
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The Hin recombinase specifically recognizes its DNA-binding site by means, of both major and minor groove interactions. A previous X-ray structure, together with new structures of the Hin DNA-binding domain bound to a, recombination half-site that were solved as part of the present study, have revealed that two ordered water molecules are present within the, major groove interface. In this report, we test the importance of these, waters directly by X-ray crystal structure analysis of complexes with four, mutant DNA sequences. These structures, combined with their Hin-binding, properties, provide strong support for the critical importance of one of, the intermediate waters. A lesser but demonstrable role is ascribed to the, second water molecule. The mutant structures also illustrate the prominent, roles of thymine methyls both in stabilizing intermediate waters and in, interfering with water or amino acid side chain interactions with DNA.
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The Hin recombinase specifically recognizes its DNA-binding site by means of both major and minor groove interactions. A previous X-ray structure, together with new structures of the Hin DNA-binding domain bound to a recombination half-site that were solved as part of the present study, have revealed that two ordered water molecules are present within the major groove interface. In this report, we test the importance of these waters directly by X-ray crystal structure analysis of complexes with four mutant DNA sequences. These structures, combined with their Hin-binding properties, provide strong support for the critical importance of one of the intermediate waters. A lesser but demonstrable role is ascribed to the second water molecule. The mutant structures also illustrate the prominent roles of thymine methyls both in stabilizing intermediate waters and in interfering with water or amino acid side chain interactions with DNA.
==About this Structure==
==About this Structure==
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1JKO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with TRS as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JKO OCA].
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1JKO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=TRS:'>TRS</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JKO OCA].
==Reference==
==Reference==
Testing water-mediated DNA recognition by the Hin recombinase., Chiu TK, Sohn C, Dickerson RE, Johnson RC, EMBO J. 2002 Feb 15;21(4):801-14. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11847127 11847127]
Testing water-mediated DNA recognition by the Hin recombinase., Chiu TK, Sohn C, Dickerson RE, Johnson RC, EMBO J. 2002 Feb 15;21(4):801-14. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11847127 11847127]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Chiu, T.K.]]
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[[Category: Chiu, T K.]]
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[[Category: Dickerson, R.E.]]
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[[Category: Dickerson, R E.]]
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[[Category: Johnson, R.C.]]
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[[Category: Johnson, R C.]]
[[Category: Sohn, C.]]
[[Category: Sohn, C.]]
[[Category: TRS]]
[[Category: TRS]]
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[[Category: water-mediated recognition]]
[[Category: water-mediated recognition]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:20:53 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:23:43 2008''

Revision as of 11:23, 21 February 2008


1jko, resolution 2.24Å

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Testing the Water-Mediated HIN Recombinase DNA Recognition by Systematic Mutations

Overview

The Hin recombinase specifically recognizes its DNA-binding site by means of both major and minor groove interactions. A previous X-ray structure, together with new structures of the Hin DNA-binding domain bound to a recombination half-site that were solved as part of the present study, have revealed that two ordered water molecules are present within the major groove interface. In this report, we test the importance of these waters directly by X-ray crystal structure analysis of complexes with four mutant DNA sequences. These structures, combined with their Hin-binding properties, provide strong support for the critical importance of one of the intermediate waters. A lesser but demonstrable role is ascribed to the second water molecule. The mutant structures also illustrate the prominent roles of thymine methyls both in stabilizing intermediate waters and in interfering with water or amino acid side chain interactions with DNA.

About this Structure

1JKO is a Single protein structure of sequence from [1] with as ligand. Full crystallographic information is available from OCA.

Reference

Testing water-mediated DNA recognition by the Hin recombinase., Chiu TK, Sohn C, Dickerson RE, Johnson RC, EMBO J. 2002 Feb 15;21(4):801-14. PMID:11847127

Page seeded by OCA on Thu Feb 21 13:23:43 2008

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