Structural and functional insights into an archaeal l-asparaginase obtained through the linker-less assembly of constituent domains. Corrigendum

Tomar, R.; Sharma, P.; Srivastava, A.; Bansal, S.; Ashish; Kundu, B.

doi:10.1107/S205979831502361X

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 7
Reaction mechanism at the EcAII (a) and PfA (b) catalytic triads. A common acidic residue Asp84 is present in both triads I and II of PfA, with Tyr273′ in triad I as the basic residue.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 72| Part 1| January 2016| Page 180

https://doi.org/10.1107/S205979831502361X

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