1snd
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(New page: 200px<br /><applet load="1snd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1snd, resolution 1.84Å" /> '''STAPHYLOCOCCAL NUCLE...)
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Revision as of 00:23, 21 November 2007
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STAPHYLOCOCCAL NUCLEASE DIMER CONTAINING A DELETION OF RESIDUES 114-119 COMPLEXED WITH CALCIUM CHLORIDE AND THE COMPETITIVE INHIBITOR DEOXYTHYMIDINE-3',5'-DIPHOSPHATE
Overview
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.
About this Structure
1SND is a Single protein structure of sequence from Staphylococcus aureus. Active as Micrococcal nuclease, with EC number 3.1.31.1 Full crystallographic information is available from OCA.
Reference
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
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