2b2j

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[[Image:2b2j.gif|left|200px]]
[[Image:2b2j.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2b2j |SIZE=350|CAPTION= <scene name='initialview01'>2b2j</scene>, resolution 1.85&Aring;
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The line below this paragraph, containing "STRUCTURE_2b2j", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=XE:XENON'>XE</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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or leave the SCENE parameter empty for the default display.
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|GENE= amt1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2234 Archaeoglobus fulgidus])
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|DOMAIN=
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{{STRUCTURE_2b2j| PDB=2b2j | SCENE= }}
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|RELATEDENTRY=[[2b2f|2B2F]], [[2b2h|2B2H]], [[2b2i|2B2I]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2b2j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b2j OCA], [http://www.ebi.ac.uk/pdbsum/2b2j PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2b2j RCSB]</span>
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'''Ammonium Transporter Amt-1 from A. fulgidus (Xe)'''
'''Ammonium Transporter Amt-1 from A. fulgidus (Xe)'''
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[[Category: Einsle, O.]]
[[Category: Einsle, O.]]
[[Category: Ficner, R.]]
[[Category: Ficner, R.]]
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[[Category: membrane protein]]
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[[Category: Membrane protein]]
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[[Category: transporter]]
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[[Category: Transporter]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:46:20 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:00:35 2008''
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Revision as of 16:46, 3 May 2008

Template:STRUCTURE 2b2j

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


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.

About this Structure

2B2J is a Single protein structure of sequence from Archaeoglobus fulgidus. Full crystallographic information is available from OCA.

Reference

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 Sat May 3 19:46:20 2008

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