8y98: Difference between revisions
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==Crystal structure of a heterooligomeric aminotransferase from Serratia sp. ATCC 39006, PPE-bound form== | |||
<StructureSection load='8y98' size='340' side='right'caption='[[8y98]], [[Resolution|resolution]] 2.31Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8y98]] 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=8Y98 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8Y98 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]] 2.31Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PGU:N-({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)-L-GLUTAMIC+ACID'>PGU</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=8y98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8y98 OCA], [https://pdbe.org/8y98 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8y98 RCSB], [https://www.ebi.ac.uk/pdbsum/8y98 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8y98 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A2I5T5Y7_SERS3 A0A2I5T5Y7_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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8y98" 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]] | |||
Latest revision as of 06:28, 18 December 2024
Crystal structure of a heterooligomeric aminotransferase from Serratia sp. ATCC 39006, PPE-bound form
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