PDBsum entry 2lvv

Metal binding protein

PDB id: 2lvv

Contents

Protein chain

220 a.a.

PDB id:

2lvv

Name:

Metal binding protein

Title:

Nmr structure of tb24

Structure:

Flagellar calcium-binding protein tb-24. Chain: a. Synonym: 24 kda calcimedin, 24 kda calflagin. Engineered: yes

Source:

Trypanosoma brucei brucei. Organism_taxid: 5702. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

10 models

Authors:

J.Ames

Key ref:

X.Xu et al. (2012). NMR structure of the calflagin Tb24 flagellar calcium binding protein of Trypanosoma brucei. Protein Sci, 21, 1942-1947. PubMed id: 23011904

Date:

11-Jul-12 Release date: 14-Nov-12

Protein chain

Q26680  (FCA2_TRYBB) -  Flagellar calcium-binding protein TB-24 from Trypanosoma brucei brucei

Seq: 218 a.a.

Struc: 220 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.?

Protein Sci 21:1942-1947 (2012)

PubMed id: 23011904

NMR structure of the calflagin Tb24 flagellar calcium binding protein of Trypanosoma brucei.

X.Xu, C.L.Olson, D.M.Engman, J.B.Ames.

ABSTRACT

Flagellar calcium binding proteins are expressed in a variety of trypanosomes and are potential drug targets for Chagas disease and African sleeping sickness. The flagellar calcium binding protein calflagin of Trypanosoma brucei (called Tb24) is a myristoylated and palmitoylated EF-hand protein that is targeted to the inner leaflet of the flagellar membrane. The Tb24 protein may also interact with proteins on the membrane surface that may be different from those bound to flagellar calcium binding proteins (FCaBPs) in T. cruzi. We report here the NMR structure of Tb24 that contains four EF-hand motifs bundled in a compact arrangement, similar to the overall fold of T. cruzi FCaBP (RMSD = 1.0 Å). A cluster of basic residues (K22, K25, K31, R36, and R38) located on a surface near the N-terminal myristoyl group may be important for membrane binding. Non-conserved residues on the surface of a hydrophobic groove formed by EF2 (P91, Q95, D103, and V108) and EF4 (C194, T198, K199, Q202, and V203) may serve as a target protein binding site and could have implications for membrane target recognition.