Two high-resolution structures of potato endo-1,3-β-glucanase reveal subdomain flexibility with implications for substrate binding

Acta Crystallographica Section D: Biological Crystallography

Volumn 68, Issue 6, 2012, Pages 713-723

  Wojtkowiak, Agnieszka ^a   Witek, Kamil ^b   Hennig, Jacek ^b   Jaskolski, Mariusz ^a,c  

^a ADAM MICKIEWICZ UNIVERSITY   (Poland)

^b INSTITUTE OF BIOCHEMISTRY AND BIOPHYSICS   (Poland)

^c INSTITUTE OF BIOORGANIC CHEMISTRY   (Poland)

Author keywords

crystal packing; GH17; glycoside hydrolases; His tags; pathogenesis related proteins; subdomains

Indexed keywords

GLUCAN ENDO 1,3 BETA GLUCOSIDASE;

AMINO ACID SEQUENCE; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; ENZYMOLOGY; METABOLISM; MOLECULAR GENETICS; POTATO; PROTEIN BINDING; PROTEIN SECONDARY STRUCTURE; SEQUENCE ALIGNMENT;

AMINO ACID SEQUENCE; CATALYTIC DOMAIN; GLUCAN ENDO-1,3-BETA-D-GLUCOSIDASE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; SEQUENCE ALIGNMENT; SOLANUM TUBEROSUM; SUBSTRATE SPECIFICITY;

EID: 84862178103     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S090744491200995X     Document Type: Article

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