PDBsum entry 2m9f

Isomerase

PDB id: 2m9f

Contents

Protein chain

33 a.a.

Ligands

NAG

PDB id:

2m9f

Name:

Isomerase

Title:

Nmr solution structure of pin1 ww domain mutant 5-1g

Structure:

Peptidyl-prolyl cis-trans isomerase nima-interacting 1. Chain: a. Fragment: modified ww domain (unp residues 6-39, see remark 999). Synonym: peptidyl-prolyl cis-trans isomerase pin1, ppiase pin1, rotamase pin1. Engineered: yes

Source:

Synthetic: yes. Homo sapiens. Human. Organism_taxid: 9606

NMR struc:

20 models

Authors:

S.Enck,W.Chen,J.L.Price,E.T.Powers,C.Wong,H.J.Dyson,J.W.Kelly

Key ref:

W.Chen et al. (2013). Structural and energetic basis of carbohydrate-aromatic packing interactions in proteins. J Am Chem Soc, 135, 9877-9884. PubMed id: 23742246 DOI: 10.1021/ja4040472

Date:

07-Jun-13 Release date: 26-Jun-13

Protein chain

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

Seq: 163 a.a.

Struc: 33 a.a.*

* PDB and UniProt seqs differ at 5 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: 10.1021/ja4040472

J Am Chem Soc 135:9877-9884 (2013)

PubMed id: 23742246

Structural and energetic basis of carbohydrate-aromatic packing interactions in proteins.

W.Chen, S.Enck, J.L.Price, D.L.Powers, E.T.Powers, C.H.Wong, H.J.Dyson, J.W.Kelly.

ABSTRACT

Carbohydrate-aromatic interactions mediate many biological processes. However, the structure-energy relationships underpinning direct carbohydrate-aromatic packing interactions in aqueous solution have been difficult to assess experimentally and remain elusive. Here, we determine the structures and folding energetics of chemically synthesized glycoproteins to quantify the contributions of the hydrophobic effect and CH-π interactions to carbohydrate-aromatic packing interactions in proteins. We find that the hydrophobic effect contributes significantly to protein-carbohydrate interactions. Interactions between carbohydrates and aromatic amino acid side chains, however, are supplemented by CH-π interactions. The strengths of experimentally determined carbohydrate CH-π interactions do not correlate with the electrostatic properties of the involved aromatic residues, suggesting that the electrostatic component of CH-π interactions in aqueous solution is small. Thus, tight binding of carbohydrates and aromatic residues is driven by the hydrophobic effect and CH-π interactions featuring a dominating dispersive component.