View source for 9upq


==Structure of 3-amino-3-carboxyltransferase==
<StructureSection load='9upq' size='340' side='right'caption='[[9upq]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9upq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Nocardia_uniformis_subsp._tsuyamanensis Nocardia uniformis subsp. tsuyamanensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9UPQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9UPQ 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]] 1.75&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=9upq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9upq OCA], [https://pdbe.org/9upq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9upq RCSB], [https://www.ebi.ac.uk/pdbsum/9upq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9upq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NAT_NOCUT NAT_NOCUT] Involved in the biosynthesis of the beta-lactam antibiotic nocardicin A (PubMed:9804844). In the presence of S-adenosyl-L-methionine (AdoMet), catalyzes the transfer of a 3-amino-3-carboxypropyl group from AdoMet to nocardicin G, forming isonocardicin C (PubMed:9804844). Can also catalyze the transformation of nocardicin E and F to isonocardicin A and B, respectively, but in vivo substrate is probably nocardicin G (PubMed:9804844).<ref>PMID:9804844</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
S-Adenosyl-l-methionine (SAM) is well-known as a methyl donor for methyltransferases but also functions as a 3-amino-3-carboxypropyl (3-ACP) donor for 3-ACP transferases. NAT is a 3-ACP transferase which accepts beta-lactam antibiotic nocardicin G (1) and SAM to produce isonocardicin C. Due to the lack of structural information about this enzyme, its reaction mechanism has not been fully identified. In this study, we report two X-ray crystal structures of NAT, including its apo and complex structure with 1 and SAH. Examination of them identified the structural basis for substrate recognition. Comprehensive approach integrating site-directed mutagenesis, thermal shift assay, MD simulation, and QM/MM calculation revealed that the Calpha-amino group of SAM functions as a Bronsted base to enhance the nucleophilicity of the C6'-OH of 1, with the assistance of E143, thereby facilitating S(N)2 attack on the Cgamma of SAM. This study presents structural and computational analysis leading to more precise understanding of 3-ACP transfer.

Structural Basis for 3-Amino-3-carboxypropyl Transfer in Nocardicin Biosynthesis.,Gao Y, Karasawa M, Quan Z, Mori T, Kanaida M, Townsend CA, Terada T, Abe I, Awakawa T J Am Chem Soc. 2025 Sep 17;147(37):33589-33596. doi: 10.1021/jacs.5c08367. Epub , 2025 Sep 8. PMID:40921178<ref>PMID:40921178</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9upq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Nocardia uniformis subsp. tsuyamanensis]]
[[Category: Abe I]]
[[Category: Awakawa T]]
[[Category: Gao Y]]
[[Category: Mori T]]