4hpp: Difference between revisions
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New page: '''Unreleased structure''' The entry 4hpp is ON HOLD Authors: Ladner, J.E., Atanasova, V., Dolezelova, Z., Parsons, J.F. Description: Crystal structure of novel glutamine synthase homo... |
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The | ==Crystal structure of novel glutamine synthase homolog== | ||
<StructureSection load='4hpp' size='340' side='right'caption='[[4hpp]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4hpp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HPP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HPP 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]] 2.5Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=4hpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hpp OCA], [https://pdbe.org/4hpp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hpp RCSB], [https://www.ebi.ac.uk/pdbsum/4hpp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hpp ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9HT65_PSEAE Q9HT65_PSEAE] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The structure of PA5508 from Pseudomonas aeruginosa, a glutamine synthetase (GS) homologue, has been determined at 2.5 A. Surprisingly, PA5508 forms single hexameric rings rather than the stacked double rings that are characteristic of GS. The C-terminal helical thong motif that links GS rings is present in PA5508; however, it is folded back toward the core of its own polypeptide, preventing it from interacting with a second ring. Interestingly, PA5508 displays a clear preference for aromatic amine substrates. Unique aspects of the structure illustrate how the enzyme is able to catalyze reactions involving bulky amines rather than ammonia. | |||
Structure and Activity of PA5508, a Hexameric Glutamine Synthetase Homologue.,Ladner JE, Atanasova V, Dolezelova Z, Parsons JF Biochemistry. 2012 Dec 21;51(51):10121-3. doi: 10.1021/bi3014856. Epub 2012 Dec, 12. PMID:23234431<ref>PMID:23234431</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4hpp" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pseudomonas aeruginosa PAO1]] | |||
[[Category: Atanasova V]] | |||
[[Category: Dolezelova Z]] | |||
[[Category: Ladner JE]] | |||
[[Category: Parsons JF]] | |||
Latest revision as of 15:09, 20 September 2023
Crystal structure of novel glutamine synthase homolog
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