Solution structure and dynamics of ADF/cofilin from Leishmania donovani

Pathak, Prem Prakash ; Pulavarti, S. V. S. R. Krishna ; Jain, Anupam ; Sahasrabuddhe, Amogh Anant ; Gupta, Chhitar Mal ; Arora, Ashish (2010) Solution structure and dynamics of ADF/cofilin from Leishmania donovani Journal of Structural Biology, 172 (3). pp. 219-224. ISSN 1047-8477

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Leishmania donovani ADF/cofilin (LdCof) is a novel member of ADF/cofilin family. LdCof depolymerizes, but does not co-sediment with, rabbit muscle actin filaments. Its F-actin depolymerizing activity is pH independent. Further, it possesses weak F-actin severing activity. In order to better understand its characteristic properties, we have determined the solution NMR structure of LdCof and have analyzed protein backbone dynamics from 15N-relaxation measurements. The structure of LdCof possesses a conserved ADF/cofilin fold with a central mixed β -sheet consisting of six β -strands which is surrounded by five α -helices. LdCof structure has conserved G/F-actin binding site which includes the characteristic long kinked α -helix (α 3). LdCof binds to rabbit muscle ADP-G-actin with 1:1 stoichiometry (Kd ~ 0.2 μ M). The F-actin binding site is not well formed and analysis of 15N-relaxation data shows that residues in the β 4-β 5 loop region and C-terminal are relatively flexible, which seems to be a determinant for the low F-actin severing activity of LdCof.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
Keywords:NMR; Leishmania donovani; ADF/cofilin; Protein Structure; Backbone Dynamics
ID Code:85633
Deposited On:05 Mar 2012 06:44
Last Modified:05 Mar 2012 06:44

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