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Crystallization and preliminary crystallographic analysis of the type IIL restriction enzyme MmeI in complex with DNA
- Source :
- Acta crystallographica. Section F, Structural biology and crystallization communications. 67(Pt 10)
- Publication Year :
- 2011
-
Abstract
- Type IIL restriction enzymes have rejuvenated the search for user-specified DNA binding and cutting. By aligning and contrasting the highly comparable amino-acid sequences yet diverse recognition specificities across the family of enzymes, amino acids involved in DNA binding have been identified and mutated to produce alternative binding specificities. To date, the specificity of MmeI (a type IIL restriction enzyme) has successfully been altered at positions 3, 4 and 6 of the asymmetric TCCRAC (where R is a purine) DNA-recognition sequence. To further understand the structural basis of MmeI DNA-binding specificity, the enzyme has been crystallized in complex with its DNA substrate. The crystal belonged to space group P1, with unit-cell parameters a = 61.73, b = 94.96, c = 161.24 A, α = 72.79, β = 89.12, γ = 71.68°, and diffracted to 2.6 A resolution when exposed to synchrotron radiation. The structure promises to reveal the basis of MmeI DNA-binding specificity and will complement efforts to create enzymes with novel specificities.
- Subjects :
- chemistry.chemical_classification
Biophysics
Substrate (chemistry)
Plasma protein binding
DNA
Biology
Condensed Matter Physics
Crystallography, X-Ray
Biochemistry
Amino acid
Restriction enzyme
chemistry.chemical_compound
Crystallography
Enzyme
chemistry
Structural Biology
Crystallization Communications
Genetics
Deoxyribonucleases
Crystallization
Deoxyribonucleases, Type II Site-Specific
Peptide sequence
Protein Binding
Subjects
Details
- ISSN :
- 17443091
- Volume :
- 67
- Issue :
- Pt 10
- Database :
- OpenAIRE
- Journal :
- Acta crystallographica. Section F, Structural biology and crystallization communications
- Accession number :
- edsair.doi.dedup.....7c7a4708b4b85f01946d6695bad0437e