2aud: Difference between revisions
New page: left|200px<br /><applet load="2aud" size="450" color="white" frame="true" align="right" spinBox="true" caption="2aud, resolution 2.1Å" /> '''Unliganded HincII'''<... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:2aud.gif|left|200px]]<br /><applet load="2aud" size=" | [[Image:2aud.gif|left|200px]]<br /><applet load="2aud" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2aud, resolution 2.1Å" /> | caption="2aud, resolution 2.1Å" /> | ||
'''Unliganded HincII'''<br /> | '''Unliganded HincII'''<br /> | ||
==Overview== | ==Overview== | ||
The 2.1A crystal structure of the unliganded type II restriction | The 2.1A crystal structure of the unliganded type II restriction endonuclease, HincII, is described. Although the asymmetric unit contains only a single monomer, crystal lattice contacts bring two monomers together to form a dimer very similar to that found in the DNA bound form. Comparison with the published DNA bound structure reveals that the DNA binding pocket is expanded in the unliganded structure. Comparison of the unliganded and DNA liganded structures reveals a simple rotation of subunits by 11 degrees each, or 22 degrees total, to a more closed structure around the bound DNA. Comparison of this conformational change to that observed in the other type II restriction endonucleases where DNA bound and unliganded forms have both been characterized, shows considerable variation in the types of conformational changes that can occur. The conformational changes in three can be described by a simple rotation of subunits, while in two others both rotation and translation of subunits relative to one another occurs. In addition, the endonucleases having subunits that undergo the greatest amount of rotation upon DNA binding are found to be those that distort the bound DNA the least, suggesting that DNA bending may be less facile in dimers possessing greater flexibility. | ||
==About this Structure== | ==About this Structure== | ||
2AUD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. 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:// | 2AUD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. 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=2AUD OCA]. | ||
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Type II site-specific deoxyribonuclease]] | [[Category: Type II site-specific deoxyribonuclease]] | ||
[[Category: Horton, N | [[Category: Horton, N C.]] | ||
[[Category: Little, E | [[Category: Little, E J.]] | ||
[[Category: blunt cutter]] | [[Category: blunt cutter]] | ||
[[Category: dna binding]] | [[Category: dna binding]] | ||
[[Category: restriction endonuclease]] | [[Category: restriction endonuclease]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:31:08 2008'' | ||
Revision as of 17:31, 21 February 2008
|
Unliganded HincII
OverviewOverview
The 2.1A crystal structure of the unliganded type II restriction endonuclease, HincII, is described. Although the asymmetric unit contains only a single monomer, crystal lattice contacts bring two monomers together to form a dimer very similar to that found in the DNA bound form. Comparison with the published DNA bound structure reveals that the DNA binding pocket is expanded in the unliganded structure. Comparison of the unliganded and DNA liganded structures reveals a simple rotation of subunits by 11 degrees each, or 22 degrees total, to a more closed structure around the bound DNA. Comparison of this conformational change to that observed in the other type II restriction endonucleases where DNA bound and unliganded forms have both been characterized, shows considerable variation in the types of conformational changes that can occur. The conformational changes in three can be described by a simple rotation of subunits, while in two others both rotation and translation of subunits relative to one another occurs. In addition, the endonucleases having subunits that undergo the greatest amount of rotation upon DNA binding are found to be those that distort the bound DNA the least, suggesting that DNA bending may be less facile in dimers possessing greater flexibility.
About this StructureAbout this Structure
2AUD is a Single protein structure of sequence from Haemophilus influenzae. Active as Type II site-specific deoxyribonuclease, with EC number 3.1.21.4 Full crystallographic information is available from OCA.
ReferenceReference
DNA-induced conformational changes in type II restriction endonucleases: the structure of unliganded HincII., Little EJ, Horton NC, J Mol Biol. 2005 Aug 5;351(1):76-88. PMID:15993893
Page seeded by OCA on Thu Feb 21 16:31:08 2008