1m32

<table><tr><td colspan='2'>[[1m32]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M32 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M32 FirstGlance]. <br>

</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=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=POA:PHOSPHONOACETALDEHYDE'>POA</scene></td></tr>

<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/2-aminoethylphosphonate--pyruvate_transaminase 2-aminoethylphosphonate--pyruvate transaminase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.37 2.6.1.37] </span></td></tr>

[[https://www.uniprot.org/uniprot/PHNW_SALTY PHNW_SALTY]] Involved in phosphonate degradation.

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== Publication Abstract from PubMed ==

Phosphonates allow certain organisms to thrive in otherwise hostile environments, and 2-aminoethylphosphonate (AEP) is a precursor of many cellular phosphonates. AEP transaminase (AEPT) is an enzyme essential to phosphonate synthesis and degradation pathways. The crystal structure of AEP transaminase was determined by multiwavelength anomalous diffraction of 66 selenium atoms. The refined structure at 2.2 A resolution revealed an overall fold and active site location similar to those of the dimeric, two-domain structure of type I aminotransferases. The active site contains a cofactor, pyridoxal 5'-phosphate (PLP), and the product phosphonoacetaldehyde. Comparison with other type I aminotransferase structures shows that the PLP-protein interactions are conserved. Modeling of bound substrates and products reveals the structural basis for AEP recognition and the stereospecificity of proton elimination at the alpha-carbon and indicates conformational changes along the reaction pathway.

Degradation pathway of the phosphonate ciliatine: crystal structure of 2-aminoethylphosphonate transaminase.,Chen CC, Zhang H, Kim AD, Howard A, Sheldrick GM, Mariano-Dunaway D, Herzberg O Biochemistry. 2002 Nov 5;41(44):13162-9. PMID:12403617<ref>PMID:12403617</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1m32" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: 2-aminoethylphosphonate--pyruvate transaminase]]

[[Category: Chen, C C.H]]

[[Category: Herzberg, O]]

[[Category: Howard, A]]

[[Category: Kim, A D]]

[[Category: Mariano-Dunnaway, D]]

[[Category: Sheldrick, G M]]

[[Category: Zhang, H]]

[[Category: Transferase]]