Sandbox UNLPam 7
From Proteopedia
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<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | ||
- | + | The crystal structure of the GH78 family a-rhamnosidase from Klebsiella oxytoca (KoRha) has been determined at 2.7 A ° | |
- | + | resolution with rhamnose bound in the active site of the catalytic domain. Curiously, the putative catalytic acid, Asp 222, is | |
+ | preceded by an unusual non-proline cis-peptide bond which helps to project the carboxyl group into the active centre. This | ||
+ | KoRha homodimeric structure is significantly smaller than those of the other previously determined GH78 structures. | ||
+ | Nevertheless, the enzyme displays a-rhamnosidase activity when assayed in vitro, suggesting that the additional structural | ||
+ | domains found in the related enzymes are dispensible for function. | ||
== Function == | == Function == |
Revision as of 12:43, 9 December 2015
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