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==Crystal structure of L-methionine decarboxylase Q64A mutant from Streptomyces sp.590 in complexed with L- methionine methyl ester (geminal diamine form).==
<StructureSection load='7cig' size='340' side='right'caption='[[7cig]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CIG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CIG 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]] 1.45&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=G03:methyl+(2S)-2-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]-4-methylsulfanyl-butanoate'>G03</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=7cig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cig OCA], [https://pdbe.org/7cig PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cig RCSB], [https://www.ebi.ac.uk/pdbsum/7cig PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cig ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
L-Methionine decarboxylase (MetDC) from Streptomyces sp. 590 is a vitamin B6 -dependent enzyme and catalyzes the non-oxidative decarboxylation of L-methionine to produce 3-methylthiopropylamine and carbon dioxide. We present here the crystal structures of the ligand-free form of MetDC and of several enzymatic reaction intermediates. Group II amino acid decarboxylases have many residues in common around the active site but the residues surrounding the side chain of the substrate differ. Based on information obtained from the crystal structure, and mutational and biochemical experiments, we propose a key role for Gln64 in determining the substrate specificity of MetDC, and for Tyr421 as the acid catalyst that participates in protonation after the decarboxylation reaction.

Structural basis for substrate specificity of L-methionine decarboxylase.,Okawa A, Shiba T, Hayashi M, Onoue Y, Murota M, Sato D, Inagaki J, Tamura T, Harada S, Inagaki K Protein Sci. 2021 Jan 15. doi: 10.1002/pro.4027. PMID:33452696<ref>PMID:33452696</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7cig" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Harada S]]
[[Category: Hayashi M]]
[[Category: Inagaki J]]
[[Category: Inagaki K]]
[[Category: Murota M]]
[[Category: Okawa A]]
[[Category: Onoue Y]]
[[Category: Sato D]]
[[Category: Shiba T]]
[[Category: Tamura T]]