Structures of trehalose synthase from Deinococcus radiodurans reveal that a closed conformation is involved in catalysis of the intramolecular isomerization

Acta Crystallographica Section D: Biological Crystallography

Volumn 70, Issue 12, 2014, Pages 3144-3154

  Wang, Yung Lin ^a   Chow, Sih Yao ^a   Lin, Yi Ting ^a   Hsieh, Yu Chiao ^a   Lee, Guan Chiun ^b   Liaw, Shwu Huey ^a,c  

^a NATIONAL YANG MING UNIVERSITY   (Taiwan)

^b NATIONAL TAIWAN NORMAL UNIVERSITY   (Taiwan)

^c TAIPEI VETERANS GENERAL HOSPITAL   (Taiwan)

Author keywords

conformational change; enzyme mechanism; glycoside hydrolase family 13; intramolecular isomerization; trehalose synthase

Indexed keywords

DEINOCOCCUS RADIODURANS;

GLUCOSYLTRANSFERASE; MALTOSE; TREHALOSE SYNTHASE;

AMINO ACID SEQUENCE; ANTAGONISTS AND INHIBITORS; CHEMICAL STRUCTURE; CHEMISTRY; DEINOCOCCUS; ENZYME ACTIVE SITE; ENZYMOLOGY; GENETICS; ISOMERISM; METABOLISM; MOLECULAR GENETICS; POINT MUTATION; PROTEIN CONFORMATION; PROTEIN TERTIARY STRUCTURE; SEQUENCE ALIGNMENT; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; DEINOCOCCUS; GLUCOSYLTRANSFERASES; ISOMERISM; MALTOSE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; POINT MUTATION; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT;

EID: 84916926032     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S1399004714022500     Document Type: Article

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