Description
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:2.52
Classification:HYDROLASE/DNA
Release Date:2008-08-26
Deposition Date:2008-08-08
Revision Date:2011-07-13
Molecular Weight:68371.62
Macromolecule Type:Protein#DNA
Residue Count:542
Atom Site Count:4491
DOI:10.2210/pdb3e44/pdb
Abstract:
Five new structures of the Q138F HincII enzyme bound to a total of three different DNA sequences and three different metal ions (Ca(2+), Mg(2+), and Mn(2+)) are presented. While previous structures were produced from soaking Ca(2+) into preformed Q138F HincII/DNA crystals, the new structures are derived from cocrystallization with Ca(2+), Mg(2+), or Mn(2+). The Mn(2)(+)-bound structure provides the first view of a product complex of Q138F HincII with cleaved DNA. Binding studies and a crystal structure show how Ca(2+) allows trapping of a Q138F HincII complex with noncognate DNA in a catalytically incompetent conformation. Many Q138F HincII/DNA structures show asymmetry, despite the binding of a symmetric substrate by a symmetric enzyme. The various complexes are fit into a model describing the different conformations of the DNA-bound enzyme and show how DNA conformational energetics determine DNA-cleavage rates by the Q138F HincII enzyme.
Resolution:2.52
Classification:HYDROLASE/DNA
Release Date:2008-08-26
Deposition Date:2008-08-08
Revision Date:2011-07-13
Molecular Weight:68371.62
Macromolecule Type:Protein#DNA
Residue Count:542
Atom Site Count:4491
DOI:10.2210/pdb3e44/pdb
Abstract:
Five new structures of the Q138F HincII enzyme bound to a total of three different DNA sequences and three different metal ions (Ca(2+), Mg(2+), and Mn(2+)) are presented. While previous structures were produced from soaking Ca(2+) into preformed Q138F HincII/DNA crystals, the new structures are derived from cocrystallization with Ca(2+), Mg(2+), or Mn(2+). The Mn(2)(+)-bound structure provides the first view of a product complex of Q138F HincII with cleaved DNA. Binding studies and a crystal structure show how Ca(2+) allows trapping of a Q138F HincII complex with noncognate DNA in a catalytically incompetent conformation. Many Q138F HincII/DNA structures show asymmetry, despite the binding of a symmetric substrate by a symmetric enzyme. The various complexes are fit into a model describing the different conformations of the DNA-bound enzyme and show how DNA conformational energetics determine DNA-cleavage rates by the Q138F HincII enzyme.
| Date made available | 2008 |
|---|---|
| Publisher | RCSB-PDB |