View source for 4hpp


==Crystal structure of novel glutamine synthase homolog==
<StructureSection load='4hpp' size='340' side='right'caption='[[4hpp]], [[Resolution|resolution]] 2.50&Aring;' 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]] 2.5&#8491;</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&reg;/PubMed&reg;, 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]]