1ZP7

The structure of Bacillus subtilis RecU Holliday junction resolvase and its role in substrate selection and sequence specific cleavage.

Summary for 1ZP7

• Entry DOI: 10.2210/pdb1zp7/pdb
• Descriptor: Recombination protein U (2 entities in total)
• Functional Keywords: recombination, dna-binding protein, resolvase, dna binding protein
• Biological source: Bacillus subtilis
• Cellular location: Cytoplasm (Probable): P39792
• Total number of polymer chains: 2
• Total formula weight: 47990.22

Authors

McGregor, N.,Ayora, S.,Sedelnikova, S.,Carrasco, B.,Alonso, J.C.,Thaw, P.,Rafferty, J. (deposition date: 2005-05-16, release date: 2005-09-20, Last modification date: 2024-02-14)

Primary citation

McGregor, N.,Ayora, S.,Sedelnikova, S.,Carrasco, B.,Alonso, J.C.,Thaw, P.,Rafferty, J.
The Structure of Bacillus subtilis RecU Holliday Junction Resolvase and Its Role in Substrate Selection and Sequence-Specific Cleavage.
Structure, 13:1341-1351, 2005

PubMed Abstract: We have determined the structure of the enzyme RecU from Bacillus subtilis, that is the general Holliday junction resolving enzyme in Gram-positive bacteria. The enzyme fold reveals a striking similarity to a class of resolvase enzymes found in archaeal sources and members of the type II restriction endonuclease family to which they are related. The structure confirms the presence of active sites formed around clusters of acidic residues that we have also shown to bind divalent cations. Mutagenesis data presented here support the key role of certain residues. The RecU structure suggests a basis for Holliday junction selectivity and suggests how sequence-specific cleavage might be achieved. Models for a resolvase-DNA complex address how the enzyme might organize junctions into an approximately 4-fold symmetric form.

PubMed: 16154091
DOI: 10.1016/j.str.2005.05.011

Experimental method

X-RAY DIFFRACTION (2.25 Å)