PDBsum entry 1z2q

Membrane protein

PDB id: 1z2q

Contents

Protein chain

84 a.a. *

* Residue conservation analysis

PDB id:

1z2q

Name:

Membrane protein

Title:

High-resolution solution structure of the lm5-1 fyve domain from leishmania major

Structure:

Lm5-1. Chain: a. Fragment: fyve domain. Engineered: yes

Source:

Leishmania major. Organism_taxid: 5664. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

NMR struc:

21 models

Authors:

H.D.T.Mertens,J.M.Callaghan,M.J.Mcconville,P.R.Gooley

Key ref:

H.D.Mertens et al. (2007). A high-resolution solution structure of a trypanosomatid FYVE domain. Protein Sci, 16, 2552-2559. PubMed id: 17905827 DOI: 10.1110/ps.073009807

Date:

08-Mar-05 Release date: 19-Apr-05

Protein chain

No UniProt id for this chain

Struc: 84 a.a.

DOI no: 10.1110/ps.073009807

Protein Sci 16:2552-2559 (2007)

PubMed id: 17905827

A high-resolution solution structure of a trypanosomatid FYVE domain.

H.D.Mertens, J.M.Callaghan, J.D.Swarbrick, M.J.McConville, P.R.Gooley.

ABSTRACT

FYVE domain proteins play key roles in regulating membrane traffic in eukaryotic cells. The FYVE domain displays a remarkable specificity for the head group of the target lipid, phosphatidylinositol 3-phosphate (PtdIns[3]P). We have identified five putative FYVE domain proteins in the genome of the protozoan parasite Leishmania major, three of which are predicted to contain a functional PtdIns(3)P-binding site. The FYVE domain of one of these proteins, LmFYVE-1, bound PtdIns(3)P in liposome-binding assays and targeted GFP to acidified late endosomes/lysosomes in mammalian cells. The high-resolution solution structure of its N-terminal FYVE domain (LmFYVE-1[1-79]) was solved by nuclear magnetic resonance. Functionally significant clusters of residues of the LmFYVE-1 domain involved in PtdIns(3)P binding and dependence on low pH for tight binding were identified. This structure is the first trypanosomatid membrane trafficking protein to be determined and has been refined to high precision and accuracy using residual dipolar couplings.

Selected figure(s)

Figure 2.
FYVE domain of LmFYVE-1(1 --79). (A) Stereoview of LmFYVE-1(1 --79). (Blue) Structure refined against RDCs, (red) unrefined structure. (B) Cartoon representation of LmFYVE-1(1 --79) showing selected side chains. (C) Overlay of FYVE domain structures. (Red) LmFYVE-1(1 --79), (yellow) EEA1(1347 --1410), (purple) HRS(156 --218), (green) Vps27 (168 --230). (D) Overlay of FYVE domain active site showing positioning of functional residues. The EEA1-bound ITP ligand as observed in the EEA1 crystal structure is shown as a ball and stick model.

Figure 3.
Heteronuclear NMR relaxation data. The longitudinal, R[1] (A), and transverse, R[2] (B), autorelaxation rates, and ^1H-^15N NOE (C) for LmFYVE-1(1 --79) acquired at 500 MHz. Data were collected in the absence (black circles) and presence (open circles) of 1.5 mM PtdIns(3)P at a protein concentration of 0.5 mM. The sequence position of secondary structure elements is indicated.

The above figures are reprinted from an Open Access publication published by the Protein Society: Protein Sci (2007, 16, 2552-2559) copyright 2007.

Figures were selected by an automated process.