Summary for 2KVK
Entry DOI | 10.2210/pdb2kvk/pdb |
Descriptor | Actin severing and dynamics regulatory protein (1 entity in total) |
Functional Keywords | adf/cofilin, leishmania donovani, hormone |
Biological source | Leishmania donovani |
Total number of polymer chains | 1 |
Total formula weight | 16253.54 |
Authors | Pathak, P.P.,Pulavarti, S.V.,Jain, A.,Sahasrabuddhe, A.A.,Gupta, C.M.,Arora, A. (deposition date: 2010-03-16, release date: 2010-07-28, Last modification date: 2024-05-01) |
Primary citation | Pathak, P.P.,Pulavarti, S.V.S.R.,Jain, A.,Sahasrabuddhe, A.A.,Gupta, C.M.,Arora, A. Solution structure and dynamics of ADF/cofilin from Leishmania donovani J.Struct.Biol., 172:219-224, 2010 Cited by PubMed Abstract: 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 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 (α3). LdCof binds to rabbit muscle ADP-G-actin with 1:1 stoichiometry (K(d)∼0.2μM). The F-actin binding site is not well formed and analysis of (15)N-relaxation data shows that residues in the β4-β5 loop region and C-terminal are relatively flexible, which seems to be a determinant for the low F-actin severing activity of LdCof. PubMed: 20627129DOI: 10.1016/j.jsb.2010.07.001 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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