PDBsum entry 2kcj

Membrane protein

PDB id: 2kcj

Contents

Protein chain

108 a.a. *

* Residue conservation analysis

PDB id:

2kcj

Name:

Membrane protein

Title:

Solution structure of fapp1 ph domain

Structure:

Pleckstrin homology domain-containing family a member 3. Chain: a. Fragment: unp residues 1-100, ph domain. Synonym: phosphoinositol 4-phosphate adaptor protein 1, fapp-1. Engineered: yes. Mutation: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: plekha3, fapp1. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

20 models

Authors:

M.Lenoir,U.Coskun,J.James,K.Simons,M.Overduin

Key ref:

M.Lenoir et al. (2010). Structural basis of wedging the Golgi membrane by FAPP pleckstrin homology domains. Embo Rep, 11, 279-284. PubMed id: 20300118

Date:

22-Dec-08 Release date: 22-Dec-09

Protein chain

Q9HB20  (PKHA3_HUMAN) -  Pleckstrin homology domain-containing family A member 3 from Homo sapiens

Seq: 300 a.a.

Struc: 108 a.a.*

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

Enzyme reactions

• Enzyme class: E.C.?

Embo Rep 11:279-284 (2010)

PubMed id: 20300118

Structural basis of wedging the Golgi membrane by FAPP pleckstrin homology domains.

M.Lenoir, U.Coskun, M.Grzybek, X.Cao, S.B.Buschhorn, J.James, K.Simons, M.Overduin.

ABSTRACT

The mechanisms underlying Golgi targeting and vesiculation are unknown, although the responsible phosphatidylinositol 4-phosphate (PtdIns(4)P) ligand and four-phosphate-adaptor protein (FAPP) modules have been defined. The micelle-bound structure of the FAPP1 pleckstrin homology domain reveals how its prominent wedge independently tubulates Golgi membranes by leaflet penetration. Mutations compromising the exposed hydrophobicity of full-length FAPP2 abolish lipid monolayer binding and compression. The trafficking process begins with an electrostatic approach, phosphoinositide sampling and perpendicular penetration. Extensive protein contacts with PtdIns(4)P and neighbouring phospholipids reshape the bilayer and initiate tubulation through a conserved wedge with features shared by diverse protein modules.