8ht2
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Acetylornithine aminotransferase from Corynebacterium glutamicum== | |
| + | <StructureSection load='8ht2' size='340' side='right'caption='[[8ht2]], [[Resolution|resolution]] 2.65Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8ht2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_glutamicum_ATCC_13032 Corynebacterium glutamicum ATCC 13032]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HT2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HT2 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]] 2.65Å</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=8ht2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ht2 OCA], [https://pdbe.org/8ht2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ht2 RCSB], [https://www.ebi.ac.uk/pdbsum/8ht2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ht2 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ARGD_CORGL ARGD_CORGL] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The amino acids l-arginine and l-ornithine are widely used in animal feed and as health supplements and pharmaceutical compounds. In arginine biosynthesis, acetylornithine aminotransferase (AcOAT) uses pyridoxal-5'-phosphate (PLP) as a cofactor for amino group transfer. Here, we determined the crystal structures of the apo and PLP complex forms of AcOAT from Corynebacterium glutamicum (CgAcOAT). Our structural observations revealed that CgAcOAT undergoes an order-to-disorder conformational change upon binding with PLP. Additionally, we observed that unlike other AcOATs, CgAcOAT exists as a tetramer. Subsequently, we identified the key residues involved in PLP and substrate binding based on structural analysis and site-directed mutagenesis. This study might provide structural insights on CgAcOAT, which can be utilized for the development of improved l-arginine production enzymes. | ||
| - | + | Crystal Structure and Functional Characterization of Acetylornithine Aminotransferase from Corynebacterium glutamicum.,Ki D, Hong H, Kim IK, Kim KJ J Agric Food Chem. 2023 Jun 7;71(22):8471-8478. doi: 10.1021/acs.jafc.3c00659. , Epub 2023 May 25. PMID:37230944<ref>PMID:37230944</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 8ht2" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Corynebacterium glutamicum ATCC 13032]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Ki D]] | ||
| + | [[Category: Kim K-J]] | ||
Current revision
Crystal structure of Acetylornithine aminotransferase from Corynebacterium glutamicum
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