2b2h: Difference between revisions

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-[[Image:2b2h.png|left|200px]]
-<!--
+==Ammonium Transporter Amt-1 from A. fulgidus (AS)==
-The line below this paragraph, containing "STRUCTURE_2b2h", creates the "Structure Box" on the page.
+<StructureSection load='2b2h' size='340' side='right'caption='[[2b2h]], [[Resolution|resolution]] 1.54&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<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>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.54&#8491;</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>
-{{STRUCTURE_2b2h|  PDB=2b2h  |  SCENE=  }}
+</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.
-===Ammonium Transporter Amt-1 from A. fulgidus (AS)===
+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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_16214888}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 2b2h" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 16214888 is the PubMed ID number.
--->
-{{ABSTRACT_PUBMED_16214888}}
-==About this Structure==
-[[2b2h]] is a 1 chain structure of [[Ion channels (Part II)]] with sequence from [http://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].
 ==See Also==
-*[[Ion channels (Part II)]]
+*[[Ion channels 3D structures|Ion channels 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:16214888</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
 [[Category: Archaeoglobus fulgidus]]
-[[Category: Andrade, S L.A.]]
+[[Category: Large Structures]]
-[[Category: Dickmanns, A.]]
+[[Category: Andrade SLA]]
-[[Category: Einsle, O.]]
+[[Category: Dickmanns A]]
-[[Category: Ficner, R.]]
+[[Category: Einsle O]]
-[[Category: Membrane protein]]
+[[Category: Ficner R]]
-[[Category: Transport protein]]
-[[Category: Transporter]]

2b2h: Difference between revisions

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