2JV4

Structure Characterisation of PINA WW Domain and Comparison with other Group IV WW Domains, PIN1 and ESS1

Replaces:  2JM7

Summary for 2JV4

• Entry DOI: 10.2210/pdb2jv4/pdb
• NMR Information: BMRB: 15466
• Descriptor: Peptidyl-prolyl cis/trans isomerase (1 entity in total)
• Functional Keywords: ppiase domain, ww domain group iv, isomerase, rotamase
• Biological source: Emericella nidulans
• Total number of polymer chains: 1
• Total formula weight: 6256.97

Authors

Ng, C.A.,Kato, Y.,Tanokura, M.,Brownlee, R.T.C. (deposition date: 2007-09-11, release date: 2007-10-16, Last modification date: 2024-05-29)

Primary citation

Ng, C.A.,Kato, Y.,Tanokura, M.,Brownlee, R.T.C.
Structural characterisation of PinA WW domain and a comparison with other Group IV WW domains, Pin1 and Ess1
Biochim.Biophys.Acta, 1784:1208-1214, 2008

PubMed Abstract: The NMR solution structure of the PinA WW domain from Aspergillus nidulans is presented. The backbone of the PinA WW domain is composed of a triple-stranded anti-parallel beta-sheet and an alpha-helix similar to Ess1 and Pin1 without the alpha-helix linker. Large RMS deviations in Loop I were observed both from the NMR structures and molecular dynamics simulation suggest that the Loop I of PinA WW domain is flexible and solvent accessible, thus enabling it to bind the pS/pT-P motif. The WW domain in this structure are stabilised by a hydrophobic core. It is shown that the linker flexibility of PinA is restricted because of an alpha-helical structure in the linker region. The combination of NMR structural data and detailed Molecular Dynamics simulations enables a comprehensive structural and dynamic understanding of this protein.

PubMed: 18503784
DOI: 10.1016/j.bbapap.2008.04.026

Experimental method

SOLUTION NMR