1snd | pdb_00001snd

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

spinqualitylabelsall models 1snd, resolution 1.84Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1snd is a 2 chain structure with sequence from Staphylococcus aureus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.84Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function NUC_STAAU Enzyme that catalyzes the hydrolysis of both DNA and RNA at the 5' position of the phosphodiester bond. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. One-step evolution of a dimer from a monomeric protein.,Green SM, Gittis AG, Meeker AK, Lattman EE Nat Struct Biol. 1995 Sep;2(9):746-51. PMID:7552745 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Staphylococcal nuclease 3D structures

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