PDBsum entry 5cbo

Protein binding

PDB id: 5cbo

Contents

Protein chains

(+ 6 more) 176 a.a.

Waters ×34

PDB id:

5cbo

Name:

Protein binding

Title:

Fusion protein of mbp3-16 and b4 domain of protein a from staphylococcal aureus

Structure:

Mbp3-16,immunoglobulin g-binding protein a. Chain: a, b, c, d, e, f, g, h, i, j, k, l. Fragment: b4 domain (unp residues 102-153). Synonym: igg-binding protein a,staphylococcal protein a. Engineered: yes. Mutation: yes. Other_details: fusion protein of mbp3-16 and b4 domain (residues 102- 153) of protein a

Source:

Synthetic construct, staphylococcus aureus. Organism_taxid: 32630, 1280. Gene: spa. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.80Å R-factor: 0.208 R-free: 0.254

Authors:

W.H.Jeong,H.Lee,D.H.Song,J.O.Lee

Key ref:

W.H.Jeong et al. (2016). Connecting two proteins using a fusion alpha helix stabilized by a chemical cross linker. Nat Commun, 7, 11031. PubMed id: 26980593 DOI: 10.1038/ncomms11031

Date:

01-Jul-15 Release date: 30-Mar-16

Protein chains

P38507  (SPA_STAAU) -  Immunoglobulin G-binding protein A from Staphylococcus aureus

Seq: 508 a.a.

Struc: 176 a.a.*

* PDB and UniProt seqs differ at 99 residue positions (black crosses)

DOI no: 10.1038/ncomms11031

Nat Commun 7:11031 (2016)

PubMed id: 26980593

Connecting two proteins using a fusion alpha helix stabilized by a chemical cross linker.

W.H.Jeong, H.Lee, D.H.Song, J.H.Eom, S.C.Kim, H.S.Lee, H.Lee, J.O.Lee.

ABSTRACT

Building a sophisticated protein nano-assembly requires a method for linking protein components in a predictable and stable structure. Most of the cross linkers available have flexible spacers. Because of this, the linked hybrids have significant structural flexibility and the relative structure between their two components is largely unpredictable. Here we describe a method of connecting two proteins via a 'fusion α helix' formed by joining two pre-existing helices into a single extended helix. Because simple ligation of two helices does not guarantee the formation of a continuous helix, we used EY-CBS, a synthetic cross linker that has been shown to react selectively with cysteines in α-helices, to stabilize the connecting helix. Formation and stabilization of the fusion helix was confirmed by determining the crystal structures of the fusion proteins with and without bound EY-CBS. Our method should be widely applicable for linking protein building blocks to generate predictable structures.