PDBsum entry 4fbz

Membrane protein

PDB id: 4fbz

Contents

Protein chain

238 a.a.

Ligands

RET

22B

SQL

L2P

BNG ×2

SO4 ×3

Waters ×12

PDB id:

4fbz

Name:

Membrane protein

Title:

Crystal structure of deltarhodopsin from haloterrigena thermotolerans

Structure:

Deltarhodopsin. Chain: a. Engineered: yes

Source:

Haloterrigena thermotolerans. Organism_taxid: 121872. Expressed in: halobacterium salinarum. Expression_system_taxid: 2242.

Resolution:

2.70Å R-factor: 0.235 R-free: 0.261

Authors:

T.Kouyama

Key ref:

J.Zhang et al. (2013). Crystal structure of deltarhodopsin-3 from Haloterrigena thermotolerans. Proteins, 81, 1585-1592. PubMed id: 23625688 DOI: 10.1002/prot.24316

Date:

23-May-12 Release date: 15-May-13

Protein chain

I4DST7  (I4DST7_9EURY) -  Deltarhodopsin (Fragment) from Natrinema thermotolerans

Seq: 241 a.a.

Struc: 238 a.a.

DOI no: 10.1002/prot.24316

Proteins 81:1585-1592 (2013)

PubMed id: 23625688

Crystal structure of deltarhodopsin-3 from Haloterrigena thermotolerans.

J.Zhang, K.Mizuno, Y.Murata, H.Koide, M.Murakami, K.Ihara, T.Kouyama.

ABSTRACT

Deltarhodopsin, a new member of the microbial rhodopsin family, functions as a light-driven proton pump. Here, we report the three-dimensional structure of deltarhodopsin (dR3) from Haloterrigena thermotolerans at 2.7 Å resolution. A crystal belonging to space group R32 (a, b = 111.71 Å, c = 198.25 Å) was obtained by the membrane fusion method. In this crystal, dR3 forms a trimeric structure as observed for bacteriorhodopsin (bR). Structural comparison of dR with bR showed that the inner part (the proton release and uptake pathways) is highly conserved. Meanwhile, residues in the protein-protein contact region are largely altered so that the diameter of the trimeric structure at the cytoplasmic side is noticeably larger in dR3. Unlike bR, dR3 possesses a helical segment at the C-terminal region that fills the space between the AB and EF loops. A significant difference is also seen in the FG loop, which is one residue longer in dR3. Another peculiar property of dR3 is a highly crowded distribution of positively charged residues on the cytoplasmic surface, which may be relevant to a specific interaction with some cytoplasmic component.Proteins 2013; © 2013 Wiley Periodicals, Inc.