2b2h: Difference between revisions

Revision as of 18:01, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2b2h.png

Template:STRUCTURE 2b2h

Ammonium Transporter Amt-1 from A. fulgidus (AS)Ammonium Transporter Amt-1 from A. fulgidus (AS)

Template:ABSTRACT PUBMED 16214888

About this StructureAbout this Structure

2B2H is a Single protein structure of sequence from Archaeoglobus fulgidus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the archaeal ammonium transporter Amt-1 from Archaeoglobus fulgidus., Andrade SL, Dickmanns A, Ficner R, Einsle O, Proc Natl Acad Sci U S A. 2005 Oct 18;102(42):14994-9. Epub 2005 Oct 7. PMID:16214888

Page seeded by OCA on Mon Jul 28 18:00:59 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:2b2h.gif|left|200px]]
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-'''Ammonium Transporter Amt-1 from A. fulgidus (AS)'''
+===Ammonium Transporter Amt-1 from A. fulgidus (AS)===
-==Overview==
+<!--
-Ammonium transporters (Amts) are integral membrane proteins found in all kingdoms of life that fulfill an essential function in the uptake of reduced nitrogen for biosynthetic purposes. Amt-1 is one of three Amts encoded in the genome of the hyperthermophilic archaeon Archaeoglobus fulgidus. The crystal structure of Amt-1 shows a compact trimer with 11 transmembrane helices per monomer and a central channel for substrate conduction in each monomer, similar to the known crystal structure of AmtB from Escherichia coli. Xenon derivatization has been used to identify apolar regions of Amt-1, emphasizing not only the hydrophobicity of the substrate channel but also the unexpected presence of extensive internal cavities that should be detrimental for protein stability. The substrates ammonium and methylammonium have been used for cocrystallization experiments with Amt-1, but the identification of binding sites that are distinct from water positions is not unambiguous. The well ordered cytoplasmic C terminus of the protein in the Amt-1 structure has allowed for the construction of a docking model between Amt-1 and a homology model for its physiological interaction partner, the P(II) protein GlnB-1. In this model, GlnB-1 binds tightly to the cytoplasmic face of the transporter, effectively blocking conduction through the three individual substrate channels.
+The line below this paragraph, {{ABSTRACT_PUBMED_16214888}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16214888 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16214888}}
 ==About this Structure==
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 [[Category: Membrane protein]]
 [[Category: Transporter]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 19:46:09 2008''
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