Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2KVK

Solution structure of ADF/cofilin (LDCOF) from Leishmania donovani

Replaces:  2KD5
Summary for 2KVK
Entry DOI10.2210/pdb2kvk/pdb
DescriptorActin severing and dynamics regulatory protein (1 entity in total)
Functional Keywordsadf/cofilin, leishmania donovani, hormone
Biological sourceLeishmania donovani
Total number of polymer chains1
Total formula weight16253.54
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 citationPathak, 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: 20627129
DOI: 10.1016/j.jsb.2010.07.001
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

229564

PDB entries from 2025-01-01

PDB statisticsPDBj update infoContact PDBjnumon