PDBsum entry 3wh0

Isomerase

PDB id: 3wh0

Contents

Protein chain

145 a.a.

Ligands

SO4

O4B ×2

DTT

Waters ×181

PDB id:

3wh0

Name:

Isomerase

Title:

Structure of pin1 complex with 18-crown-6

Structure:

Peptidyl-prolyl cis-trans isomerase nima-interacting 1. Chain: a. Synonym: peptidyl-prolyl cis-trans isomerase pin1, ppiase pin1, rotamase pin1. Engineered: yes. Mutation: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: pin1. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.60Å R-factor: 0.212 R-free: 0.247

Authors:

C.C.Lee,C.I.Liu,W.Y.Jeng,A.H.J.Wang

Key ref:

C.C.Lee et al. (2014). Crowning proteins: modulating the protein surface properties using crown ethers. Angew Chem Int Ed Engl, 53, 13054-13058. PubMed id: 25287606 DOI: 10.1002/anie.201405664

Date:

20-Aug-13 Release date: 15-Oct-14

Protein chain

Q13526  (PIN1_HUMAN) -  Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 from Homo sapiens

Seq: 163 a.a.

Struc: 145 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.5.2.1.8 - peptidylprolyl isomerase.
• Reaction: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

DOI no: 10.1002/anie.201405664

Angew Chem Int Ed Engl 53:13054-13058 (2014)

PubMed id: 25287606

Crowning proteins: modulating the protein surface properties using crown ethers.

C.C.Lee, M.Maestre-Reyna, K.C.Hsu, H.C.Wang, C.I.Liu, W.Y.Jeng, L.L.Lin, R.Wood, C.C.Chou, J.M.Yang, A.H.Wang.

ABSTRACT

Crown ethers are small, cyclic polyethers that have found wide-spread use in phase-transfer catalysis and, to a certain degree, in protein chemistry. Crown ethers readily bind metallic and organic cations, including positively charged amino acid side chains. We elucidated the crystal structures of several protein-crown ether co-crystals grown in the presence of 18-crown-6. We then employed biophysical methods and molecular dynamics simulations to compare these complexes with the corresponding apoproteins and with similar complexes with ring-shaped low-molecular-weight polyethylene glycols. Our studies show that crown ethers can modify protein surface behavior dramatically by stabilizing either intra- or intermolecular interactions. Consequently, we propose that crown ethers can be used to modulate a wide variety of protein surface behaviors, such as oligomerization, domain-domain interactions, stabilization in organic solvents, and crystallization.