PDBsum entry: 1syb

Hydrolase(phosphoric diester)

PDB id: 1syb

Contents

Protein chain

137 a.a. *

Ligands

THP

Metals

_CA

Waters ×82

* Residue conservation analysis

PDB id:

1syb

Name:

Hydrolase(phosphoric diester)

Title:

Transfer of a beta-turn structure to a new protein context

Structure:

Staphylococcal nuclease. Chain: a. Engineered: yes

Source:

Staphylococcus aureus. Organism_taxid: 1280

Resolution:

1.80Å R-factor: 0.160

Authors:

T.R.Hynes,R.A.Kautz,M.A.Goodman,J.F.Gill,R.O.Fox

Key ref:

T.R.Hynes et al. (1989). Transfer of a beta-turn structure to a new protein context. Nature, 339, 73-76. PubMed id: 2716830 DOI: 10.1038/339073a0

Date:

07-Jan-94 Release date: 31-Jul-94

Protein chain

P00644  (NUC_STAAU) -  Thermonuclease

Seq: 231 a.a.

Struc: 137 a.a.*

* PDB and UniProt seqs differ at 4 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.3.1.31.1 - Micrococcal nuclease.
• Reaction: Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products.

 Gene Ontology (GO) functional annotation 

• Biochemical function: nucleic acid binding (3 terms)

DOI no: 10.1038/339073a0

Nature 339:73-76 (1989)

PubMed id: 2716830

Transfer of a beta-turn structure to a new protein context.

T.R.Hynes, R.A.Kautz, M.A.Goodman, J.F.Gill, R.O.Fox.

ABSTRACT

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.