3HD6

Crystal Structure of the Human Rhesus Glycoprotein RhCG

Summary for 3HD6

• Entry DOI: 10.2210/pdb3hd6/pdb
• Related: 1u7g 2b2h 2ns1 3B9W 3B9Z 3BHS
• Descriptor: Ammonium transporter Rh type C, octyl beta-D-glucopyranoside (3 entities in total)
• Functional Keywords: ammonia, channel, rhesus, glycoprotein, transporter, membrane, structural genomics, psi-2, protein structure initiative, center for structures of membrane proteins, csmp, ammonia transport, cell membrane, transmembrane, transport, membrane protein, transport protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 54470.96

Authors

Gruswitz, F.,Chaudhary, S.,Ho, J.D.,Pezeshki, B.,Ho, C.-M.,Stroud, R.M.,Center for Structures of Membrane Proteins (CSMP) (deposition date: 2009-05-06, release date: 2009-09-01, Last modification date: 2023-09-06)

Primary citation

Gruswitz, F.,Chaudhary, S.,Ho, J.D.,Schlessinger, A.,Pezeshki, B.,Ho, C.M.,Sali, A.,Westhoff, C.M.,Stroud, R.M.
Function of human Rh based on structure of RhCG at 2.1 A.
Proc.Natl.Acad.Sci.USA, 107:9638-9643, 2010

PubMed Abstract: In humans, NH(3) transport across cell membranes is facilitated by the Rh (rhesus) family of proteins. Human Rh C glycoprotein (RhCG) forms a trimeric complex that plays an essential role in ammonia excretion and renal pH regulation. The X-ray crystallographic structure of human RhCG, determined at 2.1 A resolution, reveals the mechanism of ammonia transport. Each monomer contains 12 transmembrane helices, one more than in the bacterial homologs. Reconstituted into proteoliposomes, RhCG conducts NH(3) to raise internal pH. Models of the erythrocyte Rh complex based on our RhCG structure suggest that the erythrocytic Rh complex is composed of stochastically assembled heterotrimers of RhAG, RhD, and RhCE.

PubMed: 20457942
DOI: 10.1073/pnas.1003587107

Experimental method

X-RAY DIFFRACTION (2.1 Å)