1bsu
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(New page: 200px<br /><applet load="1bsu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bsu, resolution 2.0Å" /> '''STRUCTURAL AND ENERGE...)
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Revision as of 09:46, 20 November 2007
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STRUCTURAL AND ENERGETIC ORIGINS OF INDIRECT READOUT IN SITE-SPECIFIC DNA CLEAVAGE BY A RESTRICTION ENDONUCLEASE
Overview
Specific recognition by EcoRV endonuclease of its cognate, sharply bent, GATATC site at the center TA step occurs solely via hydrophobic, interaction with thymine methyl groups. Mechanistic kinetic analyses of, base analog-substituted DNAs at this position reveal that direct readout, provides 5 kcal mol(-1) toward specificity, with an additional 6-10 kcal, mol(-1) arising from indirect readout. Crystal structures of several base, analog complexes show that the major-groove hydrophobic contacts are, crucial to forming required divalent metal-binding sites, and that, indirect readout operates in part through the sequence-dependent, free-energy cost of unstacking the center base-pair step of the DNA.
About this Structure
1BSU is a Single protein structure of sequence from Escherichia coli with CA as ligand. Active as Type II site-specific deoxyribonuclease, with EC number 3.1.21.4 Full crystallographic information is available from OCA.
Reference
Structural and energetic origins of indirect readout in site-specific DNA cleavage by a restriction endonuclease., Martin AM, Sam MD, Reich NO, Perona JJ, Nat Struct Biol. 1999 Mar;6(3):269-77. PMID:10074946
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