1rv5
From Proteopedia
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| - | [[Image:1rv5.gif|left|200px]] | + | [[Image:1rv5.gif|left|200px]] |
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| - | '''COMPLEX OF ECORV ENDONUCLEASE WITH D(AAAGAT)/D(ATCTT)''' | + | {{Structure |
| + | |PDB= 1rv5 |SIZE=350|CAPTION= <scene name='initialview01'>1rv5</scene>, resolution 2.1Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''COMPLEX OF ECORV ENDONUCLEASE WITH D(AAAGAT)/D(ATCTT)''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1RV5 is a [ | + | 1RV5 is a [[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=1RV5 OCA]. |
==Reference== | ==Reference== | ||
| - | Role of protein-induced bending in the specificity of DNA recognition: crystal structure of EcoRV endonuclease complexed with d(AAAGAT) + d(ATCTT)., Horton NC, Perona JJ, J Mol Biol. 1998 Apr 10;277(4):779-87. PMID:[http:// | + | Role of protein-induced bending in the specificity of DNA recognition: crystal structure of EcoRV endonuclease complexed with d(AAAGAT) + d(ATCTT)., Horton NC, Perona JJ, J Mol Biol. 1998 Apr 10;277(4):779-87. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9545372 9545372] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: endonuclease ecorv/dna complex]] | [[Category: endonuclease ecorv/dna complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:56:38 2008'' |
Revision as of 11:56, 20 March 2008
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| , resolution 2.1Å | |||||||
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| Activity: | Type II site-specific deoxyribonuclease, with EC number 3.1.21.4 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
COMPLEX OF ECORV ENDONUCLEASE WITH D(AAAGAT)/D(ATCTT)
Overview
The crystal structure of EcoRV endonuclease has been determined at 2. 1 A resolution complexed to two five-base-pair DNA duplexes each containing the cognate recognition half-site. The highly localized 50 degrees bend into the major groove seen at the center TA-step of the continuous GATATC site is preserved in this discontinuous DNA complex lacking the scissile phosphates. Thus, this crystal structure provides evidence that covalent constraints associated with a continuous target site are not essential to enzyme-induced DNA bending, even when these constraints are removed directly at the locus of the bend. The scissile phosphates are also absent in the crystal structure of EcoRV bound to the non-specific site TCGCGA, which shows a straight B-like conformation. We conclude that DNA bending by EcoRV is governed only by the sequence and is not influenced by the continuity of the phosphodiester backbone. Together with other data showing that cleavable non-cognate sites are bent, these results indicate that EcoRV bends non-cognate sites differing by one or two base-pairs from GATATC, but does not bend non-specific sites that are less similar. Structural and thermodynamic considerations suggest that the sequence-dependent energy cost of DNA bending is likely to play an important role in determining the specificity of EcoRV. This differential cost is manifested at the binding step for bent non-cognate sequences and at the catalytic step for unbent non-specific sequences.
About this Structure
1RV5 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Role of protein-induced bending in the specificity of DNA recognition: crystal structure of EcoRV endonuclease complexed with d(AAAGAT) + d(ATCTT)., Horton NC, Perona JJ, J Mol Biol. 1998 Apr 10;277(4):779-87. PMID:9545372
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