3B9W

The 1.3 A resolution structure of Nitrosomonas europaea Rh50 and mechanistic implications for NH3 transport by Rhesus family proteins

Summary for 3B9W

• Entry DOI: 10.2210/pdb3b9w/pdb
• Related: 1U7G 1XQF 2B2F
• Descriptor: Ammonium transporter family, octyl beta-D-glucopyranoside, GLYCEROL, ... (4 entities in total)
• Functional Keywords: membrane protein, ammonia transport, rhesus protein, transport protein
• Biological source: Nitrosomonas europaea
• Total number of polymer chains: 1
• Total formula weight: 43167.10

Authors

Lupo, D.,Winkler, F.K. (deposition date: 2007-11-07, release date: 2007-11-20, Last modification date: 2023-11-01)

Primary citation

Lupo, D.,Li, X.D.,Durand, A.,Tomizaki, T.,Cherif-Zahar, B.,Matassi, G.,Merrick, M.,Winkler, F.K.
The 1.3-A resolution structure of Nitrosomonas europaea Rh50 and mechanistic implications for NH3 transport by Rhesus family proteins.
Proc.Natl.Acad.Sci.Usa, 104:19303-19308, 2007

PubMed Abstract: The Rhesus (Rh) proteins are a family of integral membrane proteins found throughout the animal kingdom that also occur in a number of lower eukaryotes. The significance of Rh proteins derives from their presence in the human red blood cell membrane, where they constitute the second most important group of antigens used in transfusion medicine after the ABO group. Rh proteins are related to the ammonium transport (Amt) protein family and there is considerable evidence that, like Amt proteins, they function as ammonia channels. We have now solved the structure of a rare bacterial homologue (from Nitrosomonas europaea) of human Rh50 proteins at a resolution of 1.3 A. The protein is a trimer, and analysis of its subunit interface strongly argues that all Rh proteins are likely to be homotrimers and that the human erythrocyte proteins RhAG and RhCE/D are unlikely to form heterooligomers as previously proposed. When compared with structures of bacterial Amt proteins, NeRh50 shows several distinctive features of the substrate conduction pathway that support the concept that Rh proteins have much lower ammonium affinities than Amt proteins and might potentially function bidirectionally.

PubMed: 18032606
DOI: 10.1073/pnas.0706563104

Experimental method

X-RAY DIFFRACTION (1.3 Å)