1JKO

Testing the Water-Mediated HIN Recombinase DNA Recognition by Systematic Mutations

Summary for 1JKO

• Entry DOI: 10.2210/pdb1jko/pdb
• Related: 1HCR 1IJW 1JJ6 1JJ8 1JKP 1JKQ 1JKR
• Descriptor: 5'-D(*TP*GP*TP*TP*TP*TP*TP*GP*GP*TP*AP*AP*GP*A)-3', 5'-D(*AP*TP*CP*TP*TP*AP*CP*CP*AP*AP*AP*AP*AP*C)-3', DNA-INVERTASE HIN, ... (5 entities in total)
• Functional Keywords: water-mediated recognition, protein-dna complex, hin recombinase, a10g mutant, dna binding protein-dna complex, dna binding protein/dna
• Total number of polymer chains: 3
• Total formula weight: 14726.82

Authors

Chiu, T.K.,Sohn, C.,Johnson, R.C.,Dickerson, R.E. (deposition date: 2001-07-12, release date: 2002-02-22, Last modification date: 2023-08-16)

Primary citation

Chiu, T.K.,Sohn, C.,Dickerson, R.E.,Johnson, R.C.
Testing water-mediated DNA recognition by the Hin recombinase.
EMBO J., 21:801-814, 2002

PubMed Abstract: The Hin recombinase specifically recognizes its DNA-binding site by means of both major and minor groove interactions. A previous X-ray structure, together with new structures of the Hin DNA-binding domain bound to a recombination half-site that were solved as part of the present study, have revealed that two ordered water molecules are present within the major groove interface. In this report, we test the importance of these waters directly by X-ray crystal structure analysis of complexes with four mutant DNA sequences. These structures, combined with their Hin-binding properties, provide strong support for the critical importance of one of the intermediate waters. A lesser but demonstrable role is ascribed to the second water molecule. The mutant structures also illustrate the prominent roles of thymine methyls both in stabilizing intermediate waters and in interfering with water or amino acid side chain interactions with DNA.

PubMed: 11847127
DOI: 10.1093/emboj/21.4.801

Experimental method

X-RAY DIFFRACTION (2.24 Å)