3b9w: Difference between revisions
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|PDB= 3b9w |SIZE=350|CAPTION= <scene name='initialview01'>3b9w</scene>, resolution 1.30Å | |PDB= 3b9w |SIZE=350|CAPTION= <scene name='initialview01'>3b9w</scene>, resolution 1.30Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene> | |LIGAND= <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= Rh50 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=915 Nitrosomonas europaea]) | |GENE= Rh50 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=915 Nitrosomonas europaea]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1xqf|1XQF]], [[1u7g|1U7G]], [[2b2f|2B2F]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3b9w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b9w OCA], [http://www.ebi.ac.uk/pdbsum/3b9w PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3b9w RCSB]</span> | |||
}} | }} | ||
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[[Category: Lupo, D.]] | [[Category: Lupo, D.]] | ||
[[Category: Winkler, F K.]] | [[Category: Winkler, F K.]] | ||
[[Category: ammonia transport]] | [[Category: ammonia transport]] | ||
[[Category: membrane protein]] | [[Category: membrane protein]] | ||
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[[Category: transport protein]] | [[Category: transport protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:24:28 2008'' | ||
Revision as of 05:24, 31 March 2008
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| , resolution 1.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | Rh50 (Nitrosomonas europaea) | ||||||
| Related: | 1XQF, 1U7G, 2B2F
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
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