PDBsum entry 6ff6

De novo protein

PDB id: 6ff6

Contents

Protein chain

222 a.a.

PDB id:

6ff6

Name:

De novo protein

Title:

Crystal structure of novel repeat protein bric1

Structure:

Bric1. Chain: a. Engineered: yes. Other_details: 1-99: n-terminal designed bundle. 100-104: designed loop 105-203: c-terminal designed bundle 204-228: natural capping helix from the chea hpt domain.

Source:

Synthetic construct. Organism_taxid: 32630. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

2.50Å R-factor: 0.233 R-free: 0.279

Authors:

M.Elgamacy,M.Coles,P.Ernst,H.Zhu,M.D.Hartmann,A.Plueckthun,A.N.Lupas

Key ref:

M.ElGamacy et al. (2018). An Interface-Driven Design Strategy Yields a Novel, Corrugated Protein Architecture. ACS Synth Biol, 7, 2226-2235. PubMed id: 30148951 DOI: 10.1021/acssynbio.8b00224

Date:

03-Jan-18 Release date: 05-Sep-18

Protein chain

No UniProt id for this chain

Struc: 222 a.a.

DOI no: 10.1021/acssynbio.8b00224

ACS Synth Biol 7:2226-2235 (2018)

PubMed id: 30148951

An Interface-Driven Design Strategy Yields a Novel, Corrugated Protein Architecture.

M.ElGamacy, M.Coles, P.Ernst, H.Zhu, M.D.Hartmann, A.Plückthun, A.N.Lupas.

ABSTRACT

Designing proteins with novel folds remains a major challenge, as the biophysical properties of the target fold are not known a priori and no sequence profile exists to describe its features. Therefore, most computational design efforts so far have been directed toward creating proteins that recapitulate existing folds. Here we present a strategy centered upon the design of novel intramolecular interfaces that enables the construction of a target fold from a set of starting fragments. This strategy effectively reduces the amount of computational sampling necessary to achieve an optimal sequence, without compromising the level of topological control. The solenoid architecture has been a target of extensive protein design efforts, as it provides a highly modular platform of low topological complexity. However, none of the previous efforts have attempted to depart from the natural form, which is characterized by a uniformly handed superhelical architecture. Here we aimed to design a more complex platform, abolishing the superhelicity by introducing internally alternating handedness, resulting in a novel, corrugated architecture. We employed our interface-driven strategy, designing three proteins and confirming the design by solving the structure of two examples.