1dmu

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(New page: 200px<br /><applet load="1dmu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dmu, resolution 2.2&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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'''CRYSTAL STRUCTURE OF THE RESTRICTION ENDONUCLEASE BGLI (E.C.3.1.21.4) BOUND TO ITS DNA RECOGNITION SEQUENCE'''<br />
'''CRYSTAL STRUCTURE OF THE RESTRICTION ENDONUCLEASE BGLI (E.C.3.1.21.4) BOUND TO ITS DNA RECOGNITION SEQUENCE'''<br />
==Overview==
==Overview==
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The crystal structure of the type II restriction endonuclease BglI bound, to DNA containing its specific recognition sequence has been determined at, 2.2 A resolution. This is the first structure of a restriction, endonuclease that recognizes and cleaves an interrupted DNA sequence, producing 3' overhanging ends. BglI is a homodimer that binds its specific, DNA sequence with the minor groove facing the protein. Parts of the enzyme, reach into both the major and minor grooves to contact the edges of the, bases within the recognition half-sites. The arrangement of active site, residues is strikingly similar to other restriction endonucleases, but the, co-ordination of two calcium ions at the active site gives new insight, into the catalytic mechanism. Surprisingly, the core of a BglI subunit, displays a striking similarity to subunits of EcoRV and PvuII, but the, dimer structure is dramatically different. The BglI-DNA complex, demonstrates, for the first time, that a conserved subunit fold can, dimerize in more than one way, resulting in different DNA cleavage, patterns.
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The crystal structure of the type II restriction endonuclease BglI bound to DNA containing its specific recognition sequence has been determined at 2.2 A resolution. This is the first structure of a restriction endonuclease that recognizes and cleaves an interrupted DNA sequence, producing 3' overhanging ends. BglI is a homodimer that binds its specific DNA sequence with the minor groove facing the protein. Parts of the enzyme reach into both the major and minor grooves to contact the edges of the bases within the recognition half-sites. The arrangement of active site residues is strikingly similar to other restriction endonucleases, but the co-ordination of two calcium ions at the active site gives new insight into the catalytic mechanism. Surprisingly, the core of a BglI subunit displays a striking similarity to subunits of EcoRV and PvuII, but the dimer structure is dramatically different. The BglI-DNA complex demonstrates, for the first time, that a conserved subunit fold can dimerize in more than one way, resulting in different DNA cleavage patterns.
==About this Structure==
==About this Structure==
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1DMU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with CA and BME as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1DMU OCA].
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1DMU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=BME:'>BME</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1DMU OCA].
==Reference==
==Reference==
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[[Category: Lunnen, K.]]
[[Category: Lunnen, K.]]
[[Category: Newman, M.]]
[[Category: Newman, M.]]
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[[Category: Phillips, S.E.V.]]
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[[Category: Phillips, S E.V.]]
[[Category: Schildkraut, I.]]
[[Category: Schildkraut, I.]]
[[Category: Wilson, G.]]
[[Category: Wilson, G.]]
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[[Category: protein-dna complex]]
[[Category: protein-dna complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:18:15 2008''

Revision as of 10:18, 21 February 2008


1dmu, resolution 2.2Å

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CRYSTAL STRUCTURE OF THE RESTRICTION ENDONUCLEASE BGLI (E.C.3.1.21.4) BOUND TO ITS DNA RECOGNITION SEQUENCE

Overview

The crystal structure of the type II restriction endonuclease BglI bound to DNA containing its specific recognition sequence has been determined at 2.2 A resolution. This is the first structure of a restriction endonuclease that recognizes and cleaves an interrupted DNA sequence, producing 3' overhanging ends. BglI is a homodimer that binds its specific DNA sequence with the minor groove facing the protein. Parts of the enzyme reach into both the major and minor grooves to contact the edges of the bases within the recognition half-sites. The arrangement of active site residues is strikingly similar to other restriction endonucleases, but the co-ordination of two calcium ions at the active site gives new insight into the catalytic mechanism. Surprisingly, the core of a BglI subunit displays a striking similarity to subunits of EcoRV and PvuII, but the dimer structure is dramatically different. The BglI-DNA complex demonstrates, for the first time, that a conserved subunit fold can dimerize in more than one way, resulting in different DNA cleavage patterns.

About this Structure

1DMU is a Single protein structure of sequence from Bacillus subtilis with and as ligands. Active as Type II site-specific deoxyribonuclease, with EC number 3.1.21.4 Full crystallographic information is available from OCA.

Reference

Crystal structure of restriction endonuclease BglI bound to its interrupted DNA recognition sequence., Newman M, Lunnen K, Wilson G, Greci J, Schildkraut I, Phillips SE, EMBO J. 1998 Sep 15;17(18):5466-76. PMID:9736624

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