Comparison of NMR and crystal structures highlights conformational isomerism in protein active sites

Serrano, P.; Pedrini, B.; Geralt, M.; Jaudzems, K.; Mohanty, B.; Horst, R.; Herrmann, T.; Elsliger, M.-A.; Wilson, I.A.; Wüthrich, K.

doi:10.1107/S1744309110033658

Figure 5
Backbone dihedral angles and side-chain torsion angles in the crystal structure of TM1081 and comparison with the NMR, reference NMR and reference crystal structures. (a–c) Spread of the values for the backbone dihedral angles φ and ψ in the bundles of 20 conformers representing the NMR structure (a), the reference NMR structure (b) and the reference crystal structure (c). In this presentation, the mean value in the bundles of 20 conformers is at 0°, the blue vertical bars represent the spread of the values within the bundles and the red dots indicate the deviation of the crystal structure values from the corresponding mean values for the bundle of 20 conformers. (d–f) Spread of the values for the amino-acid side-chain torsion angles, χ₁ and χ₂, in the NMR structure (d), the reference NMR structure (e) and the reference crystal structure (f). The same presentations are used as in (a)–(c). At the top of the two panels, the locations of the regular secondary structures are indicated and asterisks identify the residues with solvent accessibility below 15% in the NMR structure. Shading indicates the conserved residues in anti-σ factor antagonists, as in Fig. 9

(b).

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 66| Part 10| September 2010| Pages 1393-1405

doi:10.1107/S1744309110033658

Search term		doi		Advanced search
Author		volume	page