1gdr

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(New page: 200px<br /><applet load="1gdr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gdr, resolution 3.5&Aring;" /> '''MODEL FOR A DNA MEDIA...)
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[[Image:1gdr.gif|left|200px]]<br /><applet load="1gdr" size="350" color="white" frame="true" align="right" spinBox="true"
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caption="1gdr, resolution 3.5&Aring;" />
'''MODEL FOR A DNA MEDIATED SYNAPTIC COMPLEX SUGGESTED BY CRYSTAL PACKING OF GAMMA DELTA RESOLVASE SUBUNITS'''<br />
'''MODEL FOR A DNA MEDIATED SYNAPTIC COMPLEX SUGGESTED BY CRYSTAL PACKING OF GAMMA DELTA RESOLVASE SUBUNITS'''<br />
==Overview==
==Overview==
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The packing arrangement of the 12 subunits of intact gamma delta resolvase, in the unit cell of a hexagonal crystal form suggests a model for, site-specific recombination that involves a DNA-mediated synaptic, intermediate. The crystal structure has been determined by molecular, replacement and partially refined at 2.8/3.5 A resolution. Although the, small DNA-binding domain is disordered in these crystals, packing, considerations show that only a small region of space in the crystal could, accommodate a domain of its size. A family of related models for a, synaptic complex between two DNA duplexes and 12 monomers that are, arranged as situated in the crystal is consistent with the known topology, of the complex and the distances between the three resolvase dimer-binding, sites per DNA; further, these models place the two DNA recombination sites, in contact with each other between two resolvase dimers, implying that, strand exchange is accomplished through direct DNA-DNA interaction. A, major role postulated, then, for the resolvase protein assembly is to, stabilize a res DNA structure that is close to the topological transition, state of the reaction.
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The packing arrangement of the 12 subunits of intact gamma delta resolvase in the unit cell of a hexagonal crystal form suggests a model for site-specific recombination that involves a DNA-mediated synaptic intermediate. The crystal structure has been determined by molecular replacement and partially refined at 2.8/3.5 A resolution. Although the small DNA-binding domain is disordered in these crystals, packing considerations show that only a small region of space in the crystal could accommodate a domain of its size. A family of related models for a synaptic complex between two DNA duplexes and 12 monomers that are arranged as situated in the crystal is consistent with the known topology of the complex and the distances between the three resolvase dimer-binding sites per DNA; further, these models place the two DNA recombination sites in contact with each other between two resolvase dimers, implying that strand exchange is accomplished through direct DNA-DNA interaction. A major role postulated, then, for the resolvase protein assembly is to stabilize a res DNA structure that is close to the topological transition state of the reaction.
==About this Structure==
==About this Structure==
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1GDR 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=1GDR OCA].
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1GDR 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=1GDR OCA].
==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Rice, P.A.]]
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[[Category: Rice, P A.]]
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[[Category: Steitz, T.A.]]
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[[Category: Steitz, T A.]]
[[Category: site-specific recombinase]]
[[Category: site-specific recombinase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:58:11 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:48:57 2008''

Revision as of 10:48, 21 February 2008


1gdr, resolution 3.5Å

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MODEL FOR A DNA MEDIATED SYNAPTIC COMPLEX SUGGESTED BY CRYSTAL PACKING OF GAMMA DELTA RESOLVASE SUBUNITS

Overview

The packing arrangement of the 12 subunits of intact gamma delta resolvase in the unit cell of a hexagonal crystal form suggests a model for site-specific recombination that involves a DNA-mediated synaptic intermediate. The crystal structure has been determined by molecular replacement and partially refined at 2.8/3.5 A resolution. Although the small DNA-binding domain is disordered in these crystals, packing considerations show that only a small region of space in the crystal could accommodate a domain of its size. A family of related models for a synaptic complex between two DNA duplexes and 12 monomers that are arranged as situated in the crystal is consistent with the known topology of the complex and the distances between the three resolvase dimer-binding sites per DNA; further, these models place the two DNA recombination sites in contact with each other between two resolvase dimers, implying that strand exchange is accomplished through direct DNA-DNA interaction. A major role postulated, then, for the resolvase protein assembly is to stabilize a res DNA structure that is close to the topological transition state of the reaction.

About this Structure

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

Reference

Model for a DNA-mediated synaptic complex suggested by crystal packing of gamma delta resolvase subunits., Rice PA, Steitz TA, EMBO J. 1994 Apr 1;13(7):1514-24. PMID:8156989

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