Cap-domain closure enables diverse substrate recognition by the C2-type haloacid dehalogenase-like sugar phosphatase Plasmodium falciparum HAD1

Acta Crystallographica Section D: Biological Crystallography

Volumn 71, Issue , 2015, Pages 1824-1834

  Park, Jooyoung ^a   Guggisberg, Ann M ^a   Odom, Audrey R ^a   Tolia, Niraj H ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

C2 cap; HAD superfamily; haloacid dehalogenase; substrate specificity; sugar phosphatase

Indexed keywords

2-HALOACID DEHALOGENASE; HYDROLASE; PHOSPHATASE;

ANIMAL; CATALYSIS; CHEMISTRY; ENZYME SPECIFICITY; ENZYMOLOGY; METABOLISM; MOLECULAR MODEL; PLASMODIUM FALCIPARUM; PROTEIN CONFORMATION; X RAY CRYSTALLOGRAPHY;

ANIMALS; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; HYDROLASES; MODELS, MOLECULAR; PHOSPHORIC MONOESTER HYDROLASES; PLASMODIUM FALCIPARUM; PROTEIN CONFORMATION; SUBSTRATE SPECIFICITY;

EID: 84940843918     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S1399004715012067     Document Type: Article

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