Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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 (15)N-relaxation measurements. The structure of LdCof possesses a conserved ADF/cofilin fold with a central mixed beta-sheet consisting of six beta-strands which is surrounded by five alpha-helices. LdCof structure has conserved G/F-actin binding site which includes the characteristic long kinked alpha-helix (alpha3). LdCof binds to rabbit muscle ADP-G-actin with 1:1 stoichiometry (K(d) approximately 0.2muM). The F-actin binding site is not well formed and analysis of (15)N-relaxation data shows that residues in the beta4-beta5 loop region and C-terminal are relatively flexible, which seems to be a determinant for the low F-actin severing activity of LdCof.
Solution structure and dynamics of ADF/cofilin from Leishmania donovani.,Pathak PP, Pulavarti SV, Jain A, Sahasrabuddhe AA, Gupta CM, Arora A J Struct Biol. 2010 Jul 11. PMID:20627129[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pathak PP, Pulavarti SV, Jain A, Sahasrabuddhe AA, Gupta CM, Arora A. Solution structure and dynamics of ADF/cofilin from Leishmania donovani. J Struct Biol. 2010 Jul 11. PMID:20627129 doi:10.1016/j.jsb.2010.07.001
