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

The 1.3-A resolution structure of Nitrosomonas europaea Rh50 and mechanistic implications for NH3 transport by Rhesus family proteins. Research Abstract Details 

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The 1.3-A resolution structure of Nitrosomonas europaea Rh50 and mechanistic implications for NH3 transport by Rhesus family proteins. Abstract Text:

Domenico Lupo,Xiao-Dan Li,Anne Durand,Takashi Tomizaki,Baya Cherif-Zahar,Giorgio Matassi,Mike Merrick,Fritz K Winkler,Domenico Lupo,Xiao-Dan Li,Anne Durand,Takashi Tomizaki,Baya Cherif-Zahar,Giorgio Matassi,Mike Merrick,Fritz K Winkler,Domenico Lupo,Xiao-Dan Li,Anne Durand,Takashi Tomizaki,Baya Cherif-Zahar,Giorgio Matassi,Mike Merrick,Fritz K Winkler,

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.

The 1.3-A resolution structure of Nitrosomonas europaea Rh50 and mechanistic implications for NH3 transport by Rhesus family proteins. Publishing Authors By Initials

D Lupo,XD Li,A Durand,T Tomizaki,B Cherif-Zahar,G Matassi,M Merrick,FK Winkler,D Lupo,XD Li,A Durand,T Tomizaki,B Cherif-Zahar,G Matassi,M Merrick,FK Winkler,D Lupo,XD Li,A Durand,T Tomizaki,B Cherif-Zahar,G Matassi,M Merrick,FK Winkler,

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The 1.3-A resolution structure of Nitrosomonas europaea Rh50 and mechanistic implications for NH3 transport by Rhesus family proteins. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Proceedings of the National Academy of Sciences of

VOLUME: 104

Page Numbers: 19303-8

Journal Abbreviation: Proc. Natl. Acad. Sci. U.S.A.

ISSN: 1091-6490

DAY: 21

MONTH: 11

YEAR: 2007

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

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LANGUAGE: eng

NlmUniqueID: 7505876

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AFFILIATION: Biomolecular Research, Paul Scherrer Institut, CH-5232 Villigen, Switzerland.

Country: United States

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MEDLINETA: Proc Natl Acad Sci U S A

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