2b2h: Difference between revisions
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==Ammonium Transporter Amt-1 from A. fulgidus (AS)== | |||
<StructureSection load='2b2h' size='340' side='right'caption='[[2b2h]], [[Resolution|resolution]] 1.54Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2b2h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B2H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B2H FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.54Å</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2b2h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b2h OCA], [https://pdbe.org/2b2h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b2h RCSB], [https://www.ebi.ac.uk/pdbsum/2b2h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b2h ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/AMT1_ARCFU AMT1_ARCFU] Involved in the uptake of ammonium/ammonia (NH(4)(+)/NH(3)) (PubMed:22804733, PubMed:24958855). Transport is electrogenic (PubMed:22804733, PubMed:24958855). Transport the ammonium and methylammonium cation with high specificity (PubMed:24958855).<ref>PMID:22804733</ref> <ref>PMID:24958855</ref> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b2/2b2h_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2b2h ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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<ref>PMID:16214888</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2b2h" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Ion channels|Ion channels]] | *[[Ion channels 3D structures|Ion channels 3D structures]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Archaeoglobus fulgidus]] | [[Category: Archaeoglobus fulgidus]] | ||
[[Category: Andrade | [[Category: Large Structures]] | ||
[[Category: Dickmanns | [[Category: Andrade SLA]] | ||
[[Category: Einsle | [[Category: Dickmanns A]] | ||
[[Category: Ficner | [[Category: Einsle O]] | ||
[[Category: Ficner R]] | |||
Latest revision as of 11:19, 25 October 2023
Ammonium Transporter Amt-1 from A. fulgidus (AS)Ammonium Transporter Amt-1 from A. fulgidus (AS)
Structural highlights
FunctionAMT1_ARCFU Involved in the uptake of ammonium/ammonia (NH(4)(+)/NH(3)) (PubMed:22804733, PubMed:24958855). Transport is electrogenic (PubMed:22804733, PubMed:24958855). Transport the ammonium and methylammonium cation with high specificity (PubMed:24958855).[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedAmmonium 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. 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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