2BAM
RESTRICTION ENDONUCLEASE BAMHI COMPLEX WITH DNA AND CALCIUM IONS (PRE-REACTIVE COMPLEX).
Summary for 2BAM
Entry DOI | 10.2210/pdb2bam/pdb |
Descriptor | DNA (5'-D(*TP*AP*TP*GP*GP*AP*TP*CP*CP*AP*TP*A)-3'), PROTEIN (ENDONUCLEASE BAMHI), CALCIUM ION, ... (4 entities in total) |
Functional Keywords | phosphodiesterase, complex (endonuclease-dna), nuclease, hydrolase-dna complex, hydrolase/dna |
Biological source | Bacillus amyloliquefaciens |
Total number of polymer chains | 4 |
Total formula weight | 56607.58 |
Authors | Viadiu, H.,Aggarwal, A.K. (deposition date: 1998-08-19, release date: 1999-10-31, Last modification date: 2023-08-23) |
Primary citation | Viadiu, H.,Aggarwal, A.K. The role of metals in catalysis by the restriction endonuclease BamHI. Nat.Struct.Biol., 5:910-916, 1998 Cited by PubMed Abstract: 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. PubMed: 9783752DOI: 10.1038/2352 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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