3ta1

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A. fulgidus GlnK3, MgADP complex

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 <StructureSection load='3ta1' size='340' side='right'caption='[[3ta1]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3ta1]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Arcfu Arcfu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TA1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TA1 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3ta1]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus_DSM_4304 Archaeoglobus fulgidus DSM 4304]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TA1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TA1 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3t9z|3t9z]], [[3ta0|3ta0]], [[3ta2|3ta2]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AF_1750, glnK3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224325 ARCFU])</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=3ta1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ta1 OCA], [https://pdbe.org/3ta1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ta1 RCSB], [https://www.ebi.ac.uk/pdbsum/3ta1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ta1 ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/GLNK3_ARCFU GLNK3_ARCFU] Involved in the regulation of nitrogen metabolism (By similarity). Regulates the activity of its targets by protein-protein interaction in response to the nitrogen status of the cell (By similarity). Regulates the activity of the ammonia channel Amt3 via direct interaction (Probable).[UniProtKB:Q60381]<ref>PMID:22039461</ref>
-GlnK proteins regulate the active uptake of ammonium by Amt transport proteins by inserting their regulatory T-loops into the transport channels of the Amt trimer and physically blocking substrate passage. They sense the cellular nitrogen status through 2-oxoglutarate, and the energy level of the cell by binding both ATP and ADP with different affinities. The hyperthermophilic euryarchaeon Archaeoglobus fulgidus possesses three Amt proteins, each encoded in an operon with a GlnK ortholog. One of these proteins, GlnK2 was recently found to be incapable of binding 2-OG, and in order to understand the implications of this finding we conducted a detailed structural and functional analysis of a second GlnK protein from A. fulgidus, GlnK3. Contrary to Af-GlnK2 this protein was able to bind both ATP/2-OG and ADP to yield inactive and functional states, respectively. Due to the thermostable nature of the protein we could observe the exact positioning of the notoriously flexible T-loops and explain the binding behavior of GlnK proteins to their interaction partner, the Amt proteins. A thermodynamic analysis of these binding events using microcalorimetry evaluated by microstate modeling revealed significant differences in binding cooperativity compared to other characterized P(II) proteins, underlining the diversity and adaptability of this class of regulatory signaling proteins.
-Mechanism of disruption of the Amt-GlnK complex by P(II)-mediated sensing of 2-oxoglutarate.,Maier S, Schleberger P, Lu W, Wacker T, Pfluger T, Litz C, Andrade SL PLoS One. 2011;6(10):e26327. Epub 2011 Oct 19. PMID:22039461<ref>PMID:22039461</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3ta1" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Arcfu]]
+[[Category: Archaeoglobus fulgidus DSM 4304]]
 [[Category: Large Structures]]
-[[Category: Andrade, S L.A]]
+[[Category: Andrade SLA]]
-[[Category: Litz, C]]
+[[Category: Litz C]]
-[[Category: Lue, W]]
+[[Category: Lue W]]
-[[Category: Maier, S]]
+[[Category: Maier S]]
-[[Category: Pflueger, T]]
+[[Category: Pflueger T]]
-[[Category: Schleberger, P]]
+[[Category: Schleberger P]]
-[[Category: Wacker, T]]
+[[Category: Wacker T]]
-[[Category: Amt3]]
-[[Category: Pii-family]]
-[[Category: Regulator]]
-[[Category: Signaling protein]]

3ta1

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A. fulgidus GlnK3, MgADP complex

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