3bam
From Proteopedia
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[[Image:3bam.gif|left|200px]] | [[Image:3bam.gif|left|200px]] | ||
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'''RESTRICTION ENDONUCLEASE BAMHI COMPLEX WITH DNA AND MANGANESE IONS (POST-REACTIVE COMPLEX)''' | '''RESTRICTION ENDONUCLEASE BAMHI COMPLEX WITH DNA AND MANGANESE IONS (POST-REACTIVE COMPLEX)''' | ||
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[[Category: Aggarwal, A K.]] | [[Category: Aggarwal, A K.]] | ||
[[Category: Viadiu, H.]] | [[Category: Viadiu, H.]] | ||
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- | [[Category: | + | [[Category: Phosphodiesterase]] |
- | [[Category: | + | [[Category: Protein/dna]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:34:48 2008'' | |
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Revision as of 17:34, 4 May 2008
RESTRICTION ENDONUCLEASE BAMHI COMPLEX WITH DNA AND MANGANESE IONS (POST-REACTIVE COMPLEX)
Overview
Type II restriction enzymes are characterized by their remarkable specificity and simplicity. They require only divalent metals (such as Mg2+ or Mn2+) as cofactors to catalyze the hydrolysis of DNA. However, most of the structural work on endonucleases has been performed in the absence of metals, leaving unanswered questions about their mechanisms of DNA cleavage. Here we report structures of the endonuclease BamHI-DNA complex, determined in the presence of Mn2+ and Ca2+, that describe the enzyme at different stages of catalysis. Overall, the results support a two-metal mechanism of DNA cleavage for BamHI which is distinct from that of EcoRV.
About this Structure
3BAM is a Single protein structure of sequence from Bacillus amyloliquefaciens. Full crystallographic information is available from OCA.
Reference
The role of metals in catalysis by the restriction endonuclease BamHI., Viadiu H, Aggarwal AK, Nat Struct Biol. 1998 Oct;5(10):910-6. PMID:9783752 Page seeded by OCA on Sun May 4 20:34:48 2008