1syb
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(New page: 200px<br /><applet load="1syb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1syb, resolution 1.8Å" /> '''TRANSFER OF A BETA-TU...)
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Revision as of 00:43, 21 November 2007
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TRANSFER OF A BETA-TURN STRUCTURE TO A NEW PROTEIN CONTEXT
Overview
Four-residue beta-turns and larger loop structures represent a significant, fraction of globular protein surfaces and play an important role in, determining the conformation and specificity of enzyme active sites and, antibody-combining sites. Turns are an attractive starting point to, develop protein design methods, as they involve a small number of, consecutive residues, adopt a limited number of defined conformations and, are minimally constrained by packing interactions with the remainder of, the protein. The ability to substitute one beta-turn geometry for another, will extend protein engineering beyond the redecoration of fixed backbone, conformations to include local restructuring and the repositioning of, surface side chains. To determine the feasibility and to examine the, effect of such a structural modification on the fold and thermodynamic, stability of a globular protein, we have substituted a five-residue turn, sequence from concanavalin A for a type I' beta-turn in staphylococcal, nuclease. The resulting hybrid protein is folded and has full nuclease, enzymatic activity but reduced thermodynamic stability. The crystal, structure of the hybrid protein reveals that the guest turn sequence, retains the conformation of the parent concanavalin A structure when, substituted in the nuclease host.
About this Structure
1SYB is a Single protein structure of sequence from Staphylococcus aureus with CA and THP as ligands. Active as Micrococcal nuclease, with EC number 3.1.31.1 Full crystallographic information is available from OCA.
Reference
Transfer of a beta-turn structure to a new protein context., Hynes TR, Kautz RA, Goodman MA, Gill JF, Fox RO, Nature. 1989 May 4;339(6219):73-6. PMID:2716830
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