Taipei Medical University

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Liu, Z.-J., Sun, Y.-J., Rose, J., Chung, Y.-J., Hsiao, C.-D., W.-R., Kuo, I., Perozich, J., Lindahl, R., Hempel, J. and B. C. Wang
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------>author=Sun,Y.-J.
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------>journal_name=Nature Structural Biology
------>paper_name=The first structure of an aldehyde dehydrogenase reveals novel interactions between NAD and the Rossmann fold.
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------>fullAbstract=The first structure of an aldehyde dehydrogenase (ALDH) is described at 2.6 A resolution. Each subunit of the dimeric enzyme contains an NAD-binding domain, a catalytic domain and a bridging domain. At the interface of these domains is a 15 A long funnel-shaped passage with a 6 x 12 A opening leading to a putative catalytic pocket. A new mode of NAD binding, which differs substantially from the classic beta-alpha-beta binding mode associated with the ~Rossmann fold~, is observed which we term the beta-alpha,beta mode. Sequence comparisons of the class 3 ALDH with other ALDHs indicate a similar polypeptide fold, novel NAD-binding mode and catalytic site for this family. A mechanism for enzymatic specificity and activity is postulated.
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------>authors=Liu, Z.-J., Sun, Y.-J., Rose, J., Chung, Y.-J., Hsiao, C.-D., W.-R., Kuo, I., Perozich, J., Lindahl, R., Hempel, J. and B. C. Wang
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------>updateTitle=The first structure of an aldehyde dehydrogenase reveals novel interactions between NAD and the Rossmann fold.
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------>publish_year=1997
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A B C D E F G H I J K L M N O P Q R S T U V W X Y Z