RESTRICTION ENDONUCLEASE BAMHI BOUND TO A NON-SPECIFIC DNA.RESTRICTION ENDONUCLEASE BAMHI BOUND TO A NON-SPECIFIC DNA.

Structural highlights

1esg is a 4 chain structure with sequence from "bacillus_amyloliquifaciens"_(sic)_fukumoto_1943 "bacillus amyloliquifaciens" (sic) fukumoto 1943. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Activity:Type II site-specific deoxyribonuclease, with EC number 3.1.21.4
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[T2BA_BACAM] Recognizes the double-stranded sequence GGATCC and cleaves after G-1.

Publication Abstract from PubMed

The central problem faced by DNA binding proteins is how to select the correct DNA sequence from the sea of nonspecific sequences in a cell. The problem is particularly acute for bacterial restriction enzymes because cleavage at an incorrect DNA site could be lethal. To understand the basis of this selectivity, we report here the crystal structure of endonuclease BamHI bound to noncognate DNA. We show that, despite only a single base pair change in the recognition sequence, the enzyme adopts an open configuration that is on the pathway between free and specifically bound forms of the enzyme. Surprisingly, the DNA drops out of the binding cleft with a total loss of base-specific and backbone contacts. Taken together, the structure provides a remarkable snapshot of an enzyme poised for linear diffusion (rather than cleavage) along the DNA.

Structure of BamHI bound to nonspecific DNA: a model for DNA sliding.,Viadiu H, Aggarwal AK Mol Cell. 2000 May;5(5):889-95. PMID:10882125[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Viadiu H, Aggarwal AK. Structure of BamHI bound to nonspecific DNA: a model for DNA sliding. Mol Cell. 2000 May;5(5):889-95. PMID:10882125

1esg, resolution 1.90Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA