1SND

STAPHYLOCOCCAL NUCLEASE DIMER CONTAINING A DELETION OF RESIDUES 114-119 COMPLEXED WITH CALCIUM CHLORIDE AND THE COMPETITIVE INHIBITOR DEOXYTHYMIDINE-3',5'-DIPHOSPHATE

Summary for 1SND

• Entry DOI: 10.2210/pdb1snd/pdb
• Descriptor: STAPHYLOCOCCAL NUCLEASE DIMER (2 entities in total)
• Functional Keywords: hydrolase, nuclease, endonuclease
• Biological source: Staphylococcus aureus
• Cellular location: Nuclease A: Secreted. Nuclease B: Membrane: P00644
• Total number of polymer chains: 2
• Total formula weight: 32253.04

Authors

Green, S.M.,Gittis, A.G.,Meeker, A.K.,Lattman, E.E. (deposition date: 1996-08-23, release date: 1997-04-21, Last modification date: 2024-05-22)

Primary citation

Green, S.M.,Gittis, A.G.,Meeker, A.K.,Lattman, E.E.
One-step evolution of a dimer from a monomeric protein.
Nat.Struct.Biol., 2:746-751, 1995

PubMed Abstract: Deletion of six amino acids in a surface loop transforms staphylococcal nuclease from a monomeric protein into a very stable dimer (Kd < 1 x 10(-8)M). A 2 A X-ray crystal structure of the dimer (R = 0.176) shows that the carboxy-terminal alpha-helix has been stripped from its normal position in one monomer and is now incorporated into the equivalent position on the adjoining monomer. This swapping creates an association interface of 2900 A 2. A second, smaller interface of 460 A 2 is also formed. The spontaneous exchange or swapping of secondary structural elements provides a simple pathway for the formation of large, stable protein/protein interfaces and may play an important role in the evolution of oligomeric proteins.

PubMed: 7552745
DOI: 10.1038/nsb0995-746

Experimental method

X-RAY DIFFRACTION (1.84 Å)