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

ABSTRACT: The recent discovery of `lytic' polysaccharide monooxygenases, copper-dependent enzymes for biomass degradation, has provided new impetus for the analysis of unusual metal-ion sites in carbohydrate-active enzymes. In this context, the CAZY family GH124 endoglucanase from Ruminiclostridium thermocellum contains an unusual metal-ion site, which was originally modelled as a Ca²⁺ site but features aspartic acid, asparagine and two histidine imidazoles as coordinating residues, which are more consistent with a transition-metal binding environment. It was sought to analyse whether the GH124 metal-ion site might accommodate other metals. It is demonstrated through thermal unfolding experiments that this metal-ion site can accommodate a range of transition metals (Fe²⁺, Cu

SUBMITTER: Urresti S 

PROVIDER: S-EPMC6096483 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature