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2BAM

RESTRICTION ENDONUCLEASE BAMHI COMPLEX WITH DNA AND CALCIUM IONS (PRE-REACTIVE COMPLEX).

Summary for 2BAM
Entry DOI10.2210/pdb2bam/pdb
DescriptorDNA (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 Keywordsphosphodiesterase, complex (endonuclease-dna), nuclease, hydrolase-dna complex, hydrolase/dna
Biological sourceBacillus amyloliquefaciens
Total number of polymer chains4
Total formula weight56607.58
Authors
Viadiu, H.,Aggarwal, A.K. (deposition date: 1998-08-19, release date: 1999-10-31, Last modification date: 2023-08-23)
Primary citationViadiu, 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: 9783752
DOI: 10.1038/2352
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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