1zp7

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(New page: 200px<br /><applet load="1zp7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zp7, resolution 2.25&Aring;" /> '''The structure of Bac...)
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[[Image:1zp7.gif|left|200px]]<br /><applet load="1zp7" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1zp7, resolution 2.25&Aring;" />
caption="1zp7, resolution 2.25&Aring;" />
'''The structure of Bacillus subtilis RecU Holliday junction resolvase and its role in substrate selection and sequence specific cleavage.'''<br />
'''The structure of Bacillus subtilis RecU Holliday junction resolvase and its role in substrate selection and sequence specific cleavage.'''<br />
==Overview==
==Overview==
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We have determined the structure of the enzyme RecU from Bacillus, subtilis, that is the general Holliday junction resolving enzyme in, Gram-positive bacteria. The enzyme fold reveals a striking similarity to a, class of resolvase enzymes found in archaeal sources and members of the, type II restriction endonuclease family to which they are related. The, structure confirms the presence of active sites formed around clusters of, acidic residues that we have also shown to bind divalent cations., Mutagenesis data presented here support the key role of certain residues., The RecU structure suggests a basis for Holliday junction selectivity and, suggests how sequence-specific cleavage might be achieved. Models for a, resolvase-DNA complex address how the enzyme might organize junctions into, an approximately 4-fold symmetric form.
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We have determined the structure of the enzyme RecU from Bacillus subtilis, that is the general Holliday junction resolving enzyme in Gram-positive bacteria. The enzyme fold reveals a striking similarity to a class of resolvase enzymes found in archaeal sources and members of the type II restriction endonuclease family to which they are related. The structure confirms the presence of active sites formed around clusters of acidic residues that we have also shown to bind divalent cations. Mutagenesis data presented here support the key role of certain residues. The RecU structure suggests a basis for Holliday junction selectivity and suggests how sequence-specific cleavage might be achieved. Models for a resolvase-DNA complex address how the enzyme might organize junctions into an approximately 4-fold symmetric form.
==About this Structure==
==About this Structure==
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1ZP7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZP7 OCA].
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1ZP7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZP7 OCA].
==Reference==
==Reference==
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[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Alonso, J.C.]]
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[[Category: Alonso, J C.]]
[[Category: Ayora, S.]]
[[Category: Ayora, S.]]
[[Category: Carrasco, B.]]
[[Category: Carrasco, B.]]
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[[Category: resolvase]]
[[Category: resolvase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:35:11 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:17:48 2008''

Revision as of 14:17, 21 February 2008


1zp7, resolution 2.25Å

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The structure of Bacillus subtilis RecU Holliday junction resolvase and its role in substrate selection and sequence specific cleavage.

Overview

We have determined the structure of the enzyme RecU from Bacillus subtilis, that is the general Holliday junction resolving enzyme in Gram-positive bacteria. The enzyme fold reveals a striking similarity to a class of resolvase enzymes found in archaeal sources and members of the type II restriction endonuclease family to which they are related. The structure confirms the presence of active sites formed around clusters of acidic residues that we have also shown to bind divalent cations. Mutagenesis data presented here support the key role of certain residues. The RecU structure suggests a basis for Holliday junction selectivity and suggests how sequence-specific cleavage might be achieved. Models for a resolvase-DNA complex address how the enzyme might organize junctions into an approximately 4-fold symmetric form.

About this Structure

1ZP7 is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference

The structure of Bacillus subtilis RecU Holliday junction resolvase and its role in substrate selection and sequence-specific cleavage., McGregor N, Ayora S, Sedelnikova S, Carrasco B, Alonso JC, Thaw P, Rafferty J, Structure. 2005 Sep;13(9):1341-51. PMID:16154091

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