PDBsum entry 4xzv

Apoptosis

PDB id: 4xzv

Contents

Protein chains

416 a.a.

142 a.a.

133 a.a.

Ligands

GLC-GLC ×4

PDB id:

4xzv

Name:

Apoptosis

Title:

Crystal structure of slmo1-triap1 complex

Structure:

Maltose-binding periplasmic protein,tp53-regulated inhibitor of apoptosis 1. Chain: a, c, e, g. Synonym: mbp,mmbp,maltodextrin-binding protein,protein 15e1.1,wf-1, p53-inducible cell-survival factor,p53csv. Engineered: yes. Protein slowmo homolog 1. Chain: b, d, f, h. Engineered: yes

Source:

Escherichia coli k-12, homo sapiens. Human. Organism_taxid: 83333, 9606. Gene: male, b4034, jw3994, triap1, 15e1.1, hspc132. Expressed in: escherichia coli. Expression_system_taxid: 562. Homo sapiens. Organism_taxid: 9606. Gene: slmo1, c18orf43.

Resolution:

3.58Å R-factor: 0.275 R-free: 0.309

Authors:

X.Miliara,J.A.Garnett,S.J.Matthews

Key ref:

X.Miliara et al. (2015). Structural insight into the TRIAP1/PRELI-like domain family of mitochondrial phospholipid transfer complexes. Embo Rep, 16, 824-835. PubMed id: 26071602 DOI: 10.15252/embr.201540229

Date:

05-Feb-15 Release date: 20-Jan-16

Protein chains

O43715  (TRIA1_HUMAN) -  TP53-regulated inhibitor of apoptosis 1 from Homo sapiens

Seq: 76 a.a.

Struc: 416 a.a.*

Protein chains

P0AEX9  (MALE_ECOLI) -  Maltose/maltodextrin-binding periplasmic protein from Escherichia coli (strain K12)

Seq: 396 a.a.

Struc: 416 a.a.*

Protein chains

Q96N28  (PLD3A_HUMAN) -  PRELI domain containing protein 3A from Homo sapiens

Seq: 172 a.a.

Struc: 142 a.a.

Protein chain

Q96N28  (PLD3A_HUMAN) -  PRELI domain containing protein 3A from Homo sapiens

Seq: 172 a.a.

Struc: 133 a.a.

* PDB and UniProt seqs differ at 13 residue positions (black crosses)

DOI no: 10.15252/embr.201540229

Embo Rep 16:824-835 (2015)

PubMed id: 26071602

Structural insight into the TRIAP1/PRELI-like domain family of mitochondrial phospholipid transfer complexes.

X.Miliara, J.A.Garnett, T.Tatsuta, F.Abid Ali, H.Baldie, I.Pérez-Dorado, P.Simpson, E.Yague, T.Langer, S.Matthews.

ABSTRACT

The composition of the mitochondrial membrane is important for its architecture and proper function. Mitochondria depend on a tightly regulated supply of phospholipid via intra-mitochondrial synthesis and by direct import from the endoplasmic reticulum. The Ups1/PRELI-like family together with its mitochondrial chaperones (TRIAP1/Mdm35) represent a unique heterodimeric lipid transfer system that is evolutionary conserved from yeast to man. Work presented here provides new atomic resolution insight into the function of a human member of this system. Crystal structures of free TRIAP1 and the TRIAP1-SLMO1 complex reveal how the PRELI domain is chaperoned during import into the intermembrane mitochondrial space. The structural resemblance of PRELI-like domain of SLMO1 with that of mammalian phoshatidylinositol transfer proteins (PITPs) suggest that they share similar lipid transfer mechanisms, in which access to a buried phospholipid-binding cavity is regulated by conformationally adaptable loops.