PDBsum entry 5c2n

Unknown function

PDB id: 5c2n

Contents

Protein chains

46 a.a.

(+ 8 more) 47 a.a.

Ligands

NAG ×15

Waters ×500

PDB id:

5c2n

Name:

Unknown function

Title:

The de novo evolutionary emergence of a symmetrical protein is shaped by folding constraints

Structure:

Beta propeller. Chain: a, b, c, d, e, f, g, h, i, j, k, l, m, n, o. Engineered: yes

Source:

Enterobacteria phage l1. Organism_taxid: 268588. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.65Å R-factor: 0.189 R-free: 0.248

Authors:

R.G.Smock,I.Yadid,O.Dym,J.Clarke,D.S.Tawfik

Key ref:

R.G.Smock et al. (2016). De Novo Evolutionary Emergence of a Symmetrical Protein Is Shaped by Folding Constraints. Cell, 164, 476-486. PubMed id: 26806127 DOI: 10.1016/j.cell.2015.12.024

Date:

16-Jun-15 Release date: 20-Jan-16

Protein chain

A0A140UHM9  (A0A140UHM9_9VIRU) -  Beta propeller from Enterobacteria phage L1

Seq: 48 a.a.

Struc: 46 a.a.

Protein chains

A0A140UHM9  (A0A140UHM9_9VIRU) -  Beta propeller from Enterobacteria phage L1

Seq: 48 a.a.

Struc: 47 a.a.

Enzyme reactions

• Enzyme class: Chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O: E.C.?

DOI no: 10.1016/j.cell.2015.12.024

Cell 164:476-486 (2016)

PubMed id: 26806127

De Novo Evolutionary Emergence of a Symmetrical Protein Is Shaped by Folding Constraints.

R.G.Smock, I.Yadid, O.Dym, J.Clarke, D.S.Tawfik.

ABSTRACT

Molecular evolution has focused on the divergence of molecular functions, yet we know little about how structurally distinct protein folds emerge de novo. We characterized the evolutionary trajectories and selection forces underlying emergence of β-propeller proteins, a globular and symmetric fold group with diverse functions. The identification of short propeller-like motifs (<50 amino acids) in natural genomes indicated that they expanded via tandem duplications to form extant propellers. We phylogenetically reconstructed 47-residue ancestral motifs that form five-bladed lectin propellers via oligomeric assembly. We demonstrate a functional trajectory of tandem duplications of these motifs leading to monomeric lectins. Foldability, i.e., higher efficiency of folding, was the main parameter leading to improved functionality along the entire evolutionary trajectory. However, folding constraints changed along the trajectory: initially, conflicts between monomer folding and oligomer assembly dominated, whereas subsequently, upon tandem duplication, tradeoffs between monomer stability and foldability took precedence.