High-resolution structures of AidH complexes provide insights into a novel catalytic mechanism for N-acyl homoserine lactonase

Gao, A.; Mei, G.; Liu, S.; Wang, P.; Tang, Q.; Liu, Y.; Wen, H.; An, X.; Zhang, L.; Yan, X.; Liang, D.

doi:10.1107/S0907444912042369

Acta Crystallographica Section D
Acta Crystallographica
Section D BIOLOGICAL CRYSTALLOGRAPHY

IUCr IT WDC

home archive editors for authors for readers submit subscribe open access

view article

Figure 4
Substrate-binding tunnel of AidH and the conformational change of the tunnel entrance. (a) Sliced-surface view of the substrate-binding tunnel. The tunnel lying between the core and cap domains is lined by hydrophobic residues and has an overall positive charge. (b) The entrance of the tunnel is located on the cap domain and surrounded by hydrophobic residues. In (a) and (b), the molecular surface is coloured according to the electrostatic potential. Positive and negative potentials are shown in blue and red, respectively. (c) The distance between Phe189 and Phe192 changes upon substrate/product binding. In panel 1, free AidH, C4-bonded AidH and C6-bonded AidH_S102G (and AidH_E219G) are shown in purple, cyan and yellow (and green), respectively. Panel 2 shows that there is no distance change in free-form AidH_S102G (orange) and AidH_E219G (grey).

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

Volume 69| Part 1| December 2013| Pages 82-91

doi:10.1107/S0907444912042369

Follow Acta Cryst. D

Search term		doi		Advanced search
Author		volume	page