PDBsum entry 7d0a

Membrane protein

PDB id: 7d0a

Contents

Protein chains

256 a.a.

263 a.a.

95 a.a.

(+ 0 more) 191 a.a.

Ligands

ADP ×2

VO4 ×2

PDB id:

7d0a

Name:

Membrane protein

Title:

Acinetobacter mlafedb complex in adp-vanadate trapped vclose conformation

Structure:

Intermembrane phospholipid transport system permease protein mlae. Chain: a, d. Engineered: yes. Abc transporter atp-binding protein. Chain: b, e. Synonym: atp-binding cassette domain-containing protein,iron(iii) abc transporter,atp-binding protein,phospholipid abc transporter atp- binding protein mlaf,toluene tolerance efflux transporter.

Source:

Acinetobacter baumannii. Organism_taxid: 470. Expressed in: escherichia coli k-12. Expression_system_taxid: 83333. Expression_system_taxid: 83333

Authors:

Y.Y.Zhang,Q.X.Fan,X.M.Chi,Q.Zhou,Y.Y.Li

Key ref:

Y.Zhang et al. (2020). Cryo-EM structures of Acinetobacter baumannii glycerophospholipid transporter. Cell Discov, 6, 86. PubMed id: 33298869 DOI: 10.1038/s41421-020-00230-5

Date:

09-Sep-20 Release date: 16-Dec-20

Protein chains

V5V9F4  (V5V9F4_ACIBA) -  Intermembrane phospholipid transport system permease protein MlaE from Acinetobacter baumannii

Seq: 258 a.a.

Struc: 256 a.a.

Protein chains

A0A086HZU3  (A0A086HZU3_ACIBA) -  ABC transporter ATP-binding protein from Acinetobacter baumannii

Seq: 272 a.a.

Struc: 263 a.a.

Protein chains

V5V9K5  (V5V9K5_ACIBA) -  Anti-sigma factor antagonist from Acinetobacter baumannii

Seq: 95 a.a.

Struc: 95 a.a.*

Protein chains

V5V921  (V5V921_ACIBA) -  ABC transporter periplasmic substrate-binding protein from Acinetobacter baumannii

Seq: 226 a.a.

Struc: 191 a.a.

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

Enzyme reactions

• Enzyme class: Chains A, B, C, D, E, F, G, H, I, J, K, L: E.C.?

DOI no: 10.1038/s41421-020-00230-5

Cell Discov 6:86 (2020)

PubMed id: 33298869

Cryo-EM structures of Acinetobacter baumannii glycerophospholipid transporter.

Y.Zhang, Q.Fan, X.Chi, Q.Zhou, Y.Li.

ABSTRACT

No abstract given.