Structural studies of the unusual metal-ion site of the GH124 endoglucanase from Ruminiclostridium thermocellum

Urresti, S.; Cartmell, A.; Liu, F.; Walton, P.H.; Davies, G.J.

doi:10.1107/S2053230X18006842

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 6
Comparison of the sugars found in the catalytic site. When co-crystallized with G3 (above, orange), two cellotrioses were found on either side of the catalytic residue, with the chains separated by several water molecules. When co-crystallized with the G5F-contaminated cellohexaose substrate (below, blue) no cleavage was found. Furthermore, the fructose unit substituted the waters that were very well defined in the previous structure.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 74| Part 8| August 2018| Pages 496-505

https://doi.org/10.1107/S2053230X18006842

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