1eop

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(New page: 200px<br /><applet load="1eop" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eop, resolution 2.60&Aring;" /> '''ECORV BOUND TO COGNA...)
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[[Image:1eop.gif|left|200px]]<br /><applet load="1eop" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1eop, resolution 2.60&Aring;" />
caption="1eop, resolution 2.60&Aring;" />
'''ECORV BOUND TO COGNATE DNA'''<br />
'''ECORV BOUND TO COGNATE DNA'''<br />
==Overview==
==Overview==
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Two new high-resolution cocrystal structures of EcoRV endonuclease bound, to DNA show that a large variation in DNA-bending angles is sampled in the, ground state binary complex. Together with previous structures, these data, reveal a contiguous series of protein conformational states delineating a, specific trajectory for the induced-fit pathway. Rotation of the, DNA-binding domains, together with movements of two symmetry-related, helices binding in the minor groove, causes base unstacking at a key, base-pair step and propagates structural changes that assemble the active, sites. These structures suggest a complex mechanism for DNA bending that, depends on forces generated by interacting protein segments, and on, selective neutralization of phosphate charges along the inner face of the, bent double helix.
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Two new high-resolution cocrystal structures of EcoRV endonuclease bound to DNA show that a large variation in DNA-bending angles is sampled in the ground state binary complex. Together with previous structures, these data reveal a contiguous series of protein conformational states delineating a specific trajectory for the induced-fit pathway. Rotation of the DNA-binding domains, together with movements of two symmetry-related helices binding in the minor groove, causes base unstacking at a key base-pair step and propagates structural changes that assemble the active sites. These structures suggest a complex mechanism for DNA bending that depends on forces generated by interacting protein segments, and on selective neutralization of phosphate charges along the inner face of the bent double helix.
==About this Structure==
==About this Structure==
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1EOP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Type_II_site-specific_deoxyribonuclease Type II site-specific deoxyribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.21.4 3.1.21.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EOP OCA].
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1EOP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Type_II_site-specific_deoxyribonuclease Type II site-specific deoxyribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.21.4 3.1.21.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EOP OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Type II site-specific deoxyribonuclease]]
[[Category: Type II site-specific deoxyribonuclease]]
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[[Category: Horton, N.C.]]
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[[Category: Horton, N C.]]
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[[Category: Perona, J.J.]]
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[[Category: Perona, J J.]]
[[Category: endonuclease]]
[[Category: endonuclease]]
[[Category: induced fit]]
[[Category: induced fit]]
[[Category: protein-dna recognition]]
[[Category: protein-dna recognition]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:10:59 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:29:58 2008''

Revision as of 10:29, 21 February 2008


1eop, resolution 2.60Å

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ECORV BOUND TO COGNATE DNA

Overview

Two new high-resolution cocrystal structures of EcoRV endonuclease bound to DNA show that a large variation in DNA-bending angles is sampled in the ground state binary complex. Together with previous structures, these data reveal a contiguous series of protein conformational states delineating a specific trajectory for the induced-fit pathway. Rotation of the DNA-binding domains, together with movements of two symmetry-related helices binding in the minor groove, causes base unstacking at a key base-pair step and propagates structural changes that assemble the active sites. These structures suggest a complex mechanism for DNA bending that depends on forces generated by interacting protein segments, and on selective neutralization of phosphate charges along the inner face of the bent double helix.

About this Structure

1EOP is a Single protein structure of sequence from Escherichia coli. Active as Type II site-specific deoxyribonuclease, with EC number 3.1.21.4 Full crystallographic information is available from OCA.

Reference

Crystallographic snapshots along a protein-induced DNA-bending pathway., Horton NC, Perona JJ, Proc Natl Acad Sci U S A. 2000 May 23;97(11):5729-34. PMID:10801972

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