Ontology highlight
ABSTRACT:
SUBMITTER: Carpena X
PROVIDER: S-EPMC2757993 | biostudies-literature | 2009 Sep
REPOSITORIES: biostudies-literature
Carpena Xavier X Vidossich Pietro P Schroettner Klarissa K Calisto Barbara M BM Banerjee Srijib S Stampler Johanna J Soudi Monika M Furtmüller Paul G PG Rovira Carme C Fita Ignacio I Obinger Christian C
The Journal of biological chemistry 20090716 38
In heme enzymes belonging to the peroxidase-cyclooxygenase superfamily the proximal histidine is in close interaction with a fully conserved asparagine. The crystal structure of a mixture of glycoforms of myeloperoxidase (MPO) purified from granules of human leukocytes prompted us to revise the orientation of this asparagine and the protonation status of the proximal histidine. The data we present contrast with previous MPO structures, but are strongly supported by molecular dynamics simulations ...[more]