View source for 8y96


==Crystal structure of a heterooligomeric aminotransferase from Serratia sp. ATCC 39006==
<StructureSection load='8y96' size='340' side='right'caption='[[8y96]], [[Resolution|resolution]] 2.84&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8y96]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Serratia_sp._ATCC_39006 Serratia sp. ATCC 39006]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8Y96 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8Y96 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]] 2.84&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=8y96 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8y96 OCA], [https://pdbe.org/8y96 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8y96 RCSB], [https://www.ebi.ac.uk/pdbsum/8y96 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8y96 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A2I5TIB4_SERS3 A0A2I5TIB4_SERS3] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Serratia sp. ATCC 39006 has two tandemly positioned genes, ser4 and ser5, both annotated as sugar aminotransferases, in a putative secondary metabolite biosynthetic gene cluster. Ser5 possesses a complete fold-type I aminotransferase fold, while Ser4 lacks the N- and C-terminal regions and a catalytically important lysine residue of fold-type I aminotransferase. We herein revealed that Ser4 and Ser5 formed a heterotetrameric complex (SerTA) with aminotransferase activity and determined the crystal structures. MD simulations and activity assays with SerTA variants indicated that residues from helix alpha-8* of inactive Ser4 are important for activity, confirming the importance of heterocomplex formation for activity. Furthermore, the structures suggest that SerTA recognizes a substrate loaded on the carrier protein.

Crystal structure of a novel heterooligomeric aminotransferase from Serratia sp. ATCC 39006 provides insights into function.,Pramono H, Yoshida A, Hirashima Y, Sone Y, Terada T, Kosono S, Nishiyama M FEBS Lett. 2024 Dec 1. doi: 10.1002/1873-3468.15068. PMID:39618122<ref>PMID:39618122</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8y96" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Serratia sp. ATCC 39006]]
[[Category: Nishiyama M]]
[[Category: Pramono H]]
[[Category: Yoshida A]]