PDBsum entry: 1syb

Hydrolase(phosphoric diester)

PDB-id: 1syb

Contents

Description

Header details

Header records

References

PROCHECK

Protein chain

137 a.a. *

Ligands

THP

Metal ions

_CA

Waters ×82

* Residue conservation analysis

Tools

Clefts Calculation

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

UniProt:

P00644 (NUC_STAAU)

Seq:

231 a.a.

Struc:

137 a.a.*

Key:	PfamA domain
Secondary structure	CATH domain

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

Enzyme class:

E.C.3.1.31.1   [IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

Reaction:

Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products.

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

Quick_links

Procheck

Clefts

Surface

Key reference

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.