PDBsum entry 4gwv

Protein binding

PDB id: 4gwv

Contents

Protein chain

33 a.a.

Ligands

FLC

Waters ×2

PDB id:

4gwv

Name:

Protein binding

Title:

Structure of racemic pin1 ww domain cocrystallized with tri-ammonium citrate

Structure:

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

Source:

Synthetic: yes. Homo sapiens. Human. Organism_taxid: 9606. Other_details: generated via solid-phase peptide synthesis

Resolution:

3.05Å R-factor: 0.212 R-free: 0.269

Authors:

D.E.Mortenson,H.G.Yun,S.H.Gellman,K.T.Forest

Key ref:

D.E.Mortenson et al. (2013). Evidence for small-molecule-mediated loop stabilization in the structure of the isolated Pin1 WW domain. Acta Crystallogr D Biol Crystallogr, 69, 2506-2512. PubMed id: 24311591 DOI: 10.1107/S090744491302444X

Date:

03-Sep-12 Release date: 16-Oct-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.

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: 10.1107/S090744491302444X

Acta Crystallogr D Biol Crystallogr 69:2506-2512 (2013)

PubMed id: 24311591

Evidence for small-molecule-mediated loop stabilization in the structure of the isolated Pin1 WW domain.

D.E.Mortenson, D.F.Kreitler, H.G.Yun, S.H.Gellman, K.T.Forest.

ABSTRACT

The human Pin1 WW domain is a small autonomously folding protein that has been useful as a model system for biophysical studies of β-sheet folding. This domain has resisted previous attempts at crystallization for X-ray diffraction studies, perhaps because of intrinsic conformational flexibility that interferes with the formation of a crystal lattice. Here, the crystal structure of the human Pin1 WW domain has been obtained via racemic crystallization in the presence of small-molecule additives. Both enantiomers of a 36-residue variant of the Pin1 WW domain were synthesized chemically, and the L- and D-polypeptides were combined to afford diffracting crystals. The structural data revealed packing interactions of small carboxylic acids, either achiral citrate or a D,L mixture of malic acid, with a mobile loop region of the WW-domain fold. These interactions with solution additives may explain our success in crystallization of this protein racemate. Molecular-dynamics simulations starting from the structure of the Pin1 WW domain suggest that the crystal structure closely resembles the conformation of this domain in solution. The structural data presented here should provide a basis for further studies of this important model system.