Warning: Undefined array key "mm" in /www/wwwroot/www.ai-bt.com/si.php on line 10 Deprecated: trim(): Passing null to parameter #1 ($string) of type string is deprecated in /www/wwwroot/www.ai-bt.com/si.php on line 10 Mechanism of ammonia transport by Amt/MEP/Rh: structure of AmtB at 1.35 A.

Literature DB >> 15361618

Mechanism of ammonia transport by Amt/MEP/Rh: structure of AmtB at 1.35 A.

Shahram Khademi¹, Joseph O'Connell, Jonathan Remis, Yaneth Robles-Colmenares, Larry J W Miercke, Robert M Stroud.

Abstract

The first structure of an ammonia channel from the Amt/MEP/Rh protein superfamily, determined to 1.35 angstrom resolution, shows it to be a channel that spans the membrane 11 times. Two structurally similar halves span the membrane with opposite polarity. Structures with and without ammonia or methyl ammonia show a vestibule that recruits NH4+/NH3, a binding site for NH4+, and a 20 angstrom-long hydrophobic channel that lowers the NH4+ pKa to below 6 and conducts NH3. Favorable interactions for NH3 are seen within the channel and use conserved histidines. Reconstitution of AmtB into vesicles shows that AmtB conducts uncharged NH3.

Entities: Chemical Gene

Mesh：

Substances：

Year: 2004 PMID： 15361618 DOI： 10.1126/science.1101952

Source DB: PubMed Journal: Science ISSN： 0036-8075 Impact factor: 47.728

Keyword Cloud
Cited

229 in total

1. Function of human Rh based on structure of RhCG at 2.1 A.

Authors: Franz Gruswitz; Sarika Chaudhary; Joseph D Ho; Avner Schlessinger; Bobak Pezeshki; Chi-Min Ho; Andrej Sali; Connie M Westhoff; Robert M Stroud
Journal: Proc Natl Acad Sci U S A Date: 2010-05-10 Impact factor: 11.205

2. Cation-leak stomatocytosis in standard schnauzers does not cosegregate with coding mutations in the RhAG, SLC4A1, or GLUT1 genes associated with human disease.

Authors: Boris E Shmukler; Alicia Rivera; David H Vandorpe; Jessica Alves; Ugo Bonfanti; Saverio Paltrinieri; Seth L Alper
Journal: Blood Cells Mol Dis Date: 2012-03-09 Impact factor: 3.039

Review 3. Structures of membrane proteins.

Authors: Kutti R Vinothkumar; Richard Henderson
Journal: Q Rev Biophys Date: 2010-02 Impact factor: 5.318

4. Control of AmtB-GlnK complex formation by intracellular levels of ATP, ADP, and 2-oxoglutarate.

Authors: Martha V Radchenko; Jeremy Thornton; Mike Merrick
Journal: J Biol Chem Date: 2010-07-18 Impact factor: 5.157

5. CrossTalk proposal: Physiological CO2 exchange can depend on membrane channels.

Authors: Gordon J Cooper; Rossana Occhipinti; Walter F Boron
Journal: J Physiol Date: 2015-11-15 Impact factor: 5.182

6. The W148L substitution in the Escherichia coli ammonium channel AmtB increases flux and indicates that the substrate is an ion.

Authors: Rebecca N Fong; Kwang-Seo Kim; Corinne Yoshihara; William B Inwood; Sydney Kustu
Journal: Proc Natl Acad Sci U S A Date: 2007-11-12 Impact factor: 11.205

Mechanism of ammonia transport by Amt/MEP/Rh: structure of AmtB at 1.35 A.

1. Function of human Rh based on structure of RhCG at 2.1 A.

2. Cation-leak stomatocytosis in standard schnauzers does not cosegregate with coding mutations in the RhAG, SLC4A1, or GLUT1 genes associated with human disease.

Review 3. Structures of membrane proteins.

4. Control of AmtB-GlnK complex formation by intracellular levels of ATP, ADP, and 2-oxoglutarate.

5. CrossTalk proposal: Physiological CO2 exchange can depend on membrane channels.

6. The W148L substitution in the Escherichia coli ammonium channel AmtB increases flux and indicates that the substrate is an ion.

7. Diel variation in ammonia excretion, glutamine levels, and hydration status in two species of terrestrial isopods.

8. Human Rhesus-associated glycoprotein mediates facilitated transport of NH(3) into red blood cells.

Review 9. Switching substrate specificity of AMT/MEP/ Rh proteins.

10. Structure and mechanism of a pentameric formate channel.