1Z2Q

High-resolution solution structure of the LM5-1 FYVE domain from Leishmania major

Summary for 1Z2Q

• Entry DOI: 10.2210/pdb1z2q/pdb
• NMR Information: BMRB: 6594
• Descriptor: LM5-1 (1 entity in total)
• Functional Keywords: membrane protein, fyve domain, zinc-finger
• Biological source: Leishmania major
• Total number of polymer chains: 1
• Total formula weight: 9169.42

Authors

Mertens, H.D.T.,Callaghan, J.M.,McConville, M.J.,Gooley, P.R. (deposition date: 2005-03-08, release date: 2005-04-19, Last modification date: 2024-05-15)

Primary citation

Mertens, H.D.T.,Callaghan, J.M.,Swarbrick, J.D.,McConville, M.J.,Gooley, P.R.
A high-resolution solution structure of a trypanosomatid FYVE domain.
Protein Sci., 16:2552-2559, 2007

PubMed 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.

PubMed: 17905827
DOI: 10.1110/ps.073009807

Experimental method

SOLUTION NMR