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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1-2
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pubmed:dateCreated |
2006-4-24
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pubmed:abstractText |
X-ray crystallography revealed a similar architecture of the ammonium transport protein AmtB from Escherichia coli and the homologous protein Amt-1 from Archaeoglobus fulgidus. Furthermore, the atomic structures suggest that the proteins conduct ammonia (NH3) rather than ammonium ions (NH4+). These findings indicate that the more than 350 members of the ammonium transporter/methylamine permease/Rhesus (Amt/Mep/Rh) protein family found in archaea, bacteria, fungi, plants and animals are ammonia-conducting channels rather than ammonium ion transporters. The essential part of these proteins is the narrow hydrophobic ammonia-conducting pore with two highly conserved histidine residues located in the middle of the pore. A specific ammonium ion binding site is found at the extracellular entry site of E. coli AmtB. E. coli AmtB and its regulator GlnK form an effective ammonium sensory system that couples intracellular gene regulation by the nitrogen control system to external changes in ammonium availability. Based on structural and functional analysis of various mutants, two conserved histidine residues were found to be essential for substrate conductance also in the functional eukaryotic ammonium transporters. The next big challenge in the field surely is to determine the atomic structure of Rh proteins.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Ammonia,
http://linkedlifedata.com/resource/pubmed/chemical/AmtB protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/Archaeal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cation Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Histidine,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Methylamines,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleotidyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/PII Nitrogen Regulatory Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Quaternary Ammonium Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/Rh-Hr Blood-Group System,
http://linkedlifedata.com/resource/pubmed/chemical/glnK protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/methylamine
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pubmed:status |
MEDLINE
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pubmed:issn |
1246-7820
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
13
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
65-9
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:16564194-Ammonia,
pubmed-meshheading:16564194-Animals,
pubmed-meshheading:16564194-Archaeal Proteins,
pubmed-meshheading:16564194-Bacterial Proteins,
pubmed-meshheading:16564194-Binding Sites,
pubmed-meshheading:16564194-Cation Transport Proteins,
pubmed-meshheading:16564194-Crystallography, X-Ray,
pubmed-meshheading:16564194-Escherichia coli Proteins,
pubmed-meshheading:16564194-Fungal Proteins,
pubmed-meshheading:16564194-Histidine,
pubmed-meshheading:16564194-Humans,
pubmed-meshheading:16564194-Hydrophobic and Hydrophilic Interactions,
pubmed-meshheading:16564194-Membrane Transport Proteins,
pubmed-meshheading:16564194-Methylamines,
pubmed-meshheading:16564194-Nucleotidyltransferases,
pubmed-meshheading:16564194-PII Nitrogen Regulatory Proteins,
pubmed-meshheading:16564194-Plant Proteins,
pubmed-meshheading:16564194-Protein Conformation,
pubmed-meshheading:16564194-Quaternary Ammonium Compounds,
pubmed-meshheading:16564194-Rh-Hr Blood-Group System,
pubmed-meshheading:16564194-Structure-Activity Relationship,
pubmed-meshheading:16564194-Substrate Specificity
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pubmed:articleTitle |
Structural and functional insights into the AmtB/Mep/Rh protein family.
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pubmed:affiliation |
Biomolecular Research, Paul Scherrer Institute, OFLC 104, CH-5232 Villigen, Switzerland. xiao.li@psi.ch
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pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
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