2M89

Solution structure of the Aha1 dimer from Colwellia psychrerythraea

Summary for 2M89

• Entry DOI: 10.2210/pdb2m89/pdb
• NMR Information: BMRB: 19235
• Descriptor: Aha1 domain protein (1 entity in total)
• Functional Keywords: domain dimer, hybrid methods, rosetta, structural genomics, unknown function, psi-biology, northeast structural genomics consortium, nesg
• Biological source: Colwellia psychrerythraea
• Total number of polymer chains: 2
• Total formula weight: 33487.89

Authors

Rossi, P.,Sgourakis, N.G.,Shi, L.,Liu, G.,Barbieri, C.M.,Lee, H.,Grant, T.D.,Luft, J.R.,Xiao, R.,Acton, T.B.,Montelione, G.T.,Snell, E.H.,Baker, D.,Lange, O.A.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2013-05-09, release date: 2013-09-04, Last modification date: 2024-05-01)

Primary citation

Rossi, P.,Shi, L.,Liu, G.,Barbieri, C.M.,Lee, H.W.,Grant, T.D.,Luft, J.R.,Xiao, R.,Acton, T.B.,Snell, E.H.,Montelione, G.T.,Baker, D.,Lange, O.F.,Sgourakis, N.G.
A hybrid NMR/SAXS-based approach for discriminating oligomeric protein interfaces using Rosetta.
Proteins, 83:309-317, 2015

PubMed Abstract: Oligomeric proteins are important targets for structure determination in solution. While in most cases the fold of individual subunits can be determined experimentally, or predicted by homology-based methods, protein-protein interfaces are challenging to determine de novo using conventional NMR structure determination protocols. Here we focus on a member of the bet-V1 superfamily, Aha1 from Colwellia psychrerythraea. This family displays a broad range of crystallographic interfaces none of which can be reconciled with the NMR and SAXS data collected for Aha1. Unlike conventional methods relying on a dense network of experimental restraints, the sparse data are used to limit conformational search during optimization of a physically realistic energy function. This work highlights a new approach for studying minor conformational changes due to structural plasticity within a single dimeric interface in solution.

PubMed: 25388768
DOI: 10.1002/prot.24719

Experimental method

SOLUTION NMR
SOLUTION SCATTERING