View source for 3o8w


==Archaeoglobus fulgidus GlnK1==
<StructureSection load='3o8w' size='340' side='right'caption='[[3o8w]], [[Resolution|resolution]] 2.28&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3o8w]] 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=3O8W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O8W 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]] 2.28&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></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=3o8w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o8w OCA], [https://pdbe.org/3o8w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o8w RCSB], [https://www.ebi.ac.uk/pdbsum/3o8w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o8w ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GLNK1_ARCFU GLNK1_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 Amt1 via direct interaction (By similarity).[UniProtKB:Q60381]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
GlnB and GlnK are ancient signalling proteins that play a crucial role in the regulation of nitrogen assimilation. Both protein types can be present in the same genome as either single or multiple copies. However, the gene product of glnK is always found in an operon together with an amt gene encoding an ammonium-transport (Amt) protein. Complex formation between GlnK and Amt blocks ammonium uptake and depends on the nitrogen level in the cell, which is regulated through the binding of specific effector molecules to GlnK. In particular, an ammonium shock to a cell culture previously starved in this nitrogen source or the binding of ATP to purified GlnK can stimulate effective complex formation. While the binding of ATP/ADP and 2-oxoglutarate (as a signal for low intracellular nitrogen) to GlnK have been reported and several GlnB/K protein structures are available, essential functional questions remain unanswered. Here, the crystal structure of A. fulgidus GlnK1 at 2.28 A resolution and a comparison with the crystal structures of other GlnK proteins, in particular with that of its paralogue GlnK2 from the same organism, is reported.

Structure of GlnK1, a signalling protein from Archaeoglobus fulgidus.,Litz C, Helfmann S, Gerhardt S, Andrade SL Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Feb 1;67(Pt, 2):178-81. Epub 2011 Jan 21. PMID:21301082<ref>PMID:21301082</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3o8w" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Archaeoglobus fulgidus]]
[[Category: Large Structures]]
[[Category: Andrade SLA]]
[[Category: Gerhardt S]]
[[Category: Helfmann S]]
[[Category: Litz C]]