1IAW

CRYSTAL STRUCTURE OF NAEI COMPLEXED WITH 17MER DNA

Summary for 1IAW

• Entry DOI: 10.2210/pdb1iaw/pdb
• Related: 1ev7
• Descriptor: 5'-D(*TP*GP*CP*CP*AP*CP*GP*CP*CP*GP*GP*CP*GP*TP*GP*GP*C)-3', TYPE II RESTRICTION ENZYME NAEI (3 entities in total)
• Functional Keywords: protein-dna complex, hydrolase-dna complex, hydrolase/dna
• Biological source: Lechevalieria aerocolonigenes
• Total number of polymer chains: 6
• Total formula weight: 91589.46

Authors

Huai, Q.,Colandene, J.D.,Topal, M.D.,Ke, H. (deposition date: 2001-03-23, release date: 2001-08-03, Last modification date: 2024-04-03)

Primary citation

Huai, Q.,Colandene, J.D.,Topal, M.D.,Ke, H.
Structure of NaeI-DNA complex reveals dual-mode DNA recognition and complete dimer rearrangement.
Nat.Struct.Biol., 8:665-669, 2001

PubMed Abstract: NaeI, a novel DNA endonuclease, shows topoisomerase and recombinase activities when a Lys residue is substituted for Leu 43. The NaeI-DNA structure demonstrates that each of the two domains of NaeI recognizes one molecule of DNA duplex. DNA recognition induces dramatic rearrangements: narrowing the binding site of the Topo domain 16 A to grip DNA, widening that of the Endo domain 8 A to encircle and bend DNA 45 degrees for cleavage, and completely rebuilding the homodimer interface. The NaeI-DNA structure presents the first example of novel recognition of two copies of one DNA sequence by two different amino acid sequences and two different structural motifs in one polypeptide.

PubMed: 11473254
DOI: 10.1038/90366

Experimental method

X-RAY DIFFRACTION (2.4 Å)