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==Crystal structure of L-methionine decarboxylase from Streptomyces sp.590 in complexed with 3-methlythiopropylamine (geminal diamine form).==
<StructureSection load='7cim' size='340' side='right'caption='[[7cim]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CIM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CIM 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]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=G0F:[6-methyl-4-[(3-methylsulfanylpropylamino)methyl]-5-oxidanyl-pyridin-3-yl]methyl+dihydrogen+phosphate'>G0F</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=7cim FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cim OCA], [https://pdbe.org/7cim PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cim RCSB], [https://www.ebi.ac.uk/pdbsum/7cim PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cim ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== 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 7cim" 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]]