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{{STRUCTURE_4add|  PDB=4add  |  SCENE=  }}
===Structural and functional study of succinyl-ornithine transaminase from E. coli===
{{ABSTRACT_PUBMED_23484010}}


==Function==
==Structural and functional study of succinyl-ornithine transaminase from E. coli==
[[http://www.uniprot.org/uniprot/ASTC_ECOLI ASTC_ECOLI]] Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase.<ref>PMID:9696779</ref>  
<StructureSection load='4add' size='340' side='right'caption='[[4add]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4add]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21 Escherichia coli BL21]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ADD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ADD 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]] 2.45&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SUO:N~2~-(3-CARBOXYPROPANOYL)-L-ORNITHINE'>SUO</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=4add FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4add OCA], [https://pdbe.org/4add PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4add RCSB], [https://www.ebi.ac.uk/pdbsum/4add PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4add ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ASTC_ECOLI ASTC_ECOLI] Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase.<ref>PMID:9696779</ref>  


==About this Structure==
==See Also==
[[4add]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ADD OCA].
*[[Aminotransferase 3D structures|Aminotransferase 3D structures]]
 
== References ==
==Reference==
<references/>
<references group="xtra"/><references/>
__TOC__
[[Category: Escherichia coli]]
</StructureSection>
[[Category: Newman, J.]]
[[Category: Escherichia coli BL21]]
[[Category: Peat, T S.]]
[[Category: Large Structures]]
[[Category: Aminotransferase]]
[[Category: Newman J]]
[[Category: Plp enzyme]]
[[Category: Peat TS]]
[[Category: Transferase]]

Latest revision as of 10:14, 1 May 2024

Structural and functional study of succinyl-ornithine transaminase from E. coliStructural and functional study of succinyl-ornithine transaminase from E. coli

Structural highlights

4add is a 4 chain structure with sequence from Escherichia coli BL21. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.45Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ASTC_ECOLI Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase.[1]

See Also

References

  1. ↑ Schneider BL, Kiupakis AK, Reitzer LJ. Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli. J Bacteriol. 1998 Aug;180(16):4278-86. PMID:9696779

4add, resolution 2.45Å

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