3b9w: Difference between revisions

Revision as of 20:04, 21 February 2008

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

OverviewOverview

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.

About this StructureAbout this Structure

3B9W is a Single protein structure of sequence from Nitrosomonas europaea with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

The 1.3-A resolution structure of Nitrosomonas europaea Rh50 and mechanistic implications for NH3 transport by Rhesus family proteins., Lupo D, Li XD, Durand A, Tomizaki T, Cherif-Zahar B, Matassi G, Merrick M, Winkler FK, Proc Natl Acad Sci U S A. 2007 Dec 4;104(49):19303-8. Epub 2007 Nov 21. PMID:18032606

Page seeded by OCA on Thu Feb 21 19:04:30 2008

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 ==Overview==
-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 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.
 ==About this Structure==
@@ Line 10: / Line 10: @@
 ==Reference==
-The 1.3-A resolution structure of Nitrosomonas europaea Rh50 and mechanistic implications for NH3 transport by Rhesus family proteins., Lupo D, Li XD, Durand A, Tomizaki T, Cherif-Zahar B, Matassi G, Merrick M, Winkler FK, Proc Natl Acad Sci U S A. 2007 Nov 21;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18032606 18032606]
+The 1.3-A resolution structure of Nitrosomonas europaea Rh50 and mechanistic implications for NH3 transport by Rhesus family proteins., Lupo D, Li XD, Durand A, Tomizaki T, Cherif-Zahar B, Matassi G, Merrick M, Winkler FK, Proc Natl Acad Sci U S A. 2007 Dec 4;104(49):19303-8. Epub 2007 Nov 21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18032606 18032606]
 [[Category: Nitrosomonas europaea]]
 [[Category: Single protein]]
 [[Category: Lupo, D.]]
-[[Category: Winkler, F.K.]]
+[[Category: Winkler, F K.]]
 [[Category: BOG]]
 [[Category: GOL]]
@@ Line 22: / Line 22: @@
 [[Category: transport protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:50:41 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:04:30 2008''