PDBsum entry 3w56

Lipid binding protein

PDB id: 3w56

Contents

Protein chain

108 a.a.

Waters ×152

PDB id:

3w56

Name:

Lipid binding protein

Title:

Structure of a c2 domain

Structure:

C2 domain protein. Chain: a. Fragment: unp residues 21-129. Synonym: smc2p1. Engineered: yes

Source:

Scophthalmus maximus. Turbot. Organism_taxid: 52904. Gene: c2p1. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.60Å R-factor: 0.214 R-free: 0.251

Authors:

D.A.K.Traore,J.C.Whisstock

Key ref:

D.A.Traore et al. (2013). Defining the interaction of perforin with calcium and the phospholipid membrane. Biochem J, 456, 323-335. PubMed id: 24070258 DOI: 10.1042/BJ20130999

Date:

24-Jan-13 Release date: 23-Oct-13

Protein chain

E2FYL5  (E2FYL5_SCOMX) -  C2 domain protein from Scophthalmus maximus

Seq: 129 a.a.

Struc: 108 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

DOI no: 10.1042/BJ20130999

Biochem J 456:323-335 (2013)

PubMed id: 24070258

Defining the interaction of perforin with calcium and the phospholipid membrane.

D.A.Traore, A.J.Brennan, R.H.Law, C.Dogovski, M.A.Perugini, N.Lukoyanova, E.W.Leung, R.S.Norton, J.A.Lopez, K.A.Browne, H.Yagita, G.J.Lloyd, A.Ciccone, S.Verschoor, J.A.Trapani, J.C.Whisstock, I.Voskoboinik.

ABSTRACT

Following its secretion from cytotoxic lymphocytes into the immune synapse, perforin binds to target cell membranes through its Ca2+-dependent C2 domain. Membrane-bound perforin then forms pores that allow passage of pro-apoptopic granzymes into the target cell. In the present study, structural and biochemical studies reveal that Ca2+ binding triggers a conformational change in the C2 domain that permits four key hydrophobic residues to interact with the plasma membrane. However, in contrast with previous suggestions, these movements and membrane binding do not trigger irreversible conformational changes in the pore-forming MACPF (membrane attack complex/perforin-like) domain, indicating that subsequent monomer-monomer interactions at the membrane surface are required for perforin pore formation.