PDBsum entry 6svh

Peptide binding protein

PDB id: 6svh

Contents

Protein chain

35 a.a.

PDB id:

6svh

Name:

Peptide binding protein

Title:

Protein allostery of the ww domain at atomic resolution: ffpspr bound structure

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 bl21(de3). Expression_system_taxid: 469008

NMR struc:

20 models

Authors:

D.Strotz,J.Orts,M.Friedmann,P.Guntert,B.Vogeli,R.Riek

Key ref:

D.Strotz et al. (2020). Protein Allostery at Atomic Resolution. Angew Chem Int Ed Engl, 59, 22132-22139. PubMed id: 32797659 DOI: 10.1002/anie.202008734

Date:

18-Sep-19 Release date: 30-Sep-20

Protein chain

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

Seq: 163 a.a.

Struc: 35 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

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.202008734

Angew Chem Int Ed Engl 59:22132-22139 (2020)

PubMed id: 32797659

Protein Allostery at Atomic Resolution.

D.Strotz, J.Orts, H.Kadavath, M.Friedmann, D.Ghosh, S.Olsson, C.N.Chi, A.Pokharna, P.Güntert, B.Vögeli, R.Riek.

ABSTRACT

Protein allostery is a phenomenon involving the long range coupling between two distal sites in a protein. In order to elucidate allostery at atomic resoluion on the ligand-binding WW domain of the enzyme Pin1, multistate structures were calculated from exact nuclear Overhauser effect (eNOE). In its free form, the protein undergoes a microsecond exchange between two states, one of which is predisposed to interact with its parent catalytic domain. In presence of the positive allosteric ligand, the equilibrium between the two states is shifted towards domain-domain interaction, suggesting a population shift model. In contrast, the allostery-suppressing ligand decouples the side-chain arrangement at the inter-domain interface thereby reducing the inter-domain interaction. As such, this mechanism is an example of dynamic allostery. The presented distinct modes of action highlight the power of the interplay between dynamics and function in the biological activity of proteins.