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[[Image:4hpp.jpg|left|200px]]
==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 [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HPP FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PA5508 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=208964 Pseudomonas aeruginosa PAO1])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate--putrescine_ligase Glutamate--putrescine ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.1.11 6.3.1.11] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4hpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hpp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hpp RCSB], [http://www.ebi.ac.uk/pdbsum/4hpp PDBsum]</span></td></tr>
</table>
<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_4hpp|  PDB=4hpp  |  SCENE=  }}
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>


===Crystal structure of novel glutamine synthase homolog===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_23234431}}
== References ==
 
<references/>
==About this Structure==
__TOC__
[[4hpp]] is a 1 chain structure with sequence from [http://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].
</StructureSection>
[[Category: Glutamate--putrescine ligase]]
[[Category: Glutamate--putrescine ligase]]
[[Category: Pseudomonas aeruginosa pao1]]
[[Category: Pseudomonas aeruginosa pao1]]
[[Category: Atanasova, V.]]
[[Category: Atanasova, V]]
[[Category: Dolezelova, Z.]]
[[Category: Dolezelova, Z]]
[[Category: Ladner, J E.]]
[[Category: Ladner, J E]]
[[Category: Parsons, J F.]]
[[Category: Parsons, J F]]
[[Category: Glutamate]]
[[Category: Glutamate]]
[[Category: Glutamine synthase homolog]]
[[Category: Glutamine synthase homolog]]
[[Category: Ligase]]
[[Category: Ligase]]
[[Category: Polyamine]]
[[Category: Polyamine]]

Revision as of 09:41, 10 December 2014

Crystal structure of novel glutamine synthase homolog

4hpp, resolution 2.50Å

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