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 | STRUCTURAL BIOLOGY |
Structural and functional insights into an archaeal L-asparaginase obtained through the linker-less assembly of constituent domains. Corrigendum
aKusuma School of Biological Sciences, Indian Institute of Technology Delhi, New Delhi, India, and bCSIR – Institute of Microbial Technology, Chandigarh, India
*Correspondence e-mail: bkundu@bioschool.iitd.ac.in
A correction is made to Fig. 7 in the article by Tomar et al. [(2014). Acta Cryst. D70, 3187–3197].
Keywords: L-asparaginase; Pyrococcus furiosus; linker-less assembly; corrigendum.
In the article by Tomar et al. (2014![[Tomar, R., Sharma, P., Srivastava, A., Bansal, S., Ashish, & Kundu, B. (2014). Acta Cryst. D70, 3187-3197.]](../../../../../../logos/arrows/d_arr.gif "Tomar, R., Sharma, P., Srivastava, A., Bansal, S., Ashish, & Kundu, B. (2014). Acta Cryst. D70, 3187-3197.")
), the product formula in Fig. 7 was incorrect. A new version of the figure with the correct formula is given here.
![[Figure 7]](qh9016fig7thm.gif) | 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. |
References
Tomar, R., Sharma, P., Srivastava, A., Bansal, S., Ashish, & Kundu, B. (2014). Acta Cryst. D70, 3187–3197. CrossRef IUCr Journals Google Scholar
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| STRUCTURAL BIOLOGY |
