View source for 7cij


==Crystal structure of L-methionine decarboxylase from Streptomyces sp.590 in complexed with 3-methlythiopropylamine (external aldimine form).==
<StructureSection load='7cij' size='340' side='right'caption='[[7cij]], [[Resolution|resolution]] 1.61&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7cij]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._590_KI-2014 Streptomyces sp. 590 KI-2014]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CIJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CIJ 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]] 1.61&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=G0C:[6-methyl-4-[(E)-3-methylsulfanylpropyliminomethyl]-5-oxidanyl-pyridin-3-yl]methyl+dihydrogen+phosphate'>G0C</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=7cij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cij OCA], [https://pdbe.org/7cij PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cij RCSB], [https://www.ebi.ac.uk/pdbsum/7cij PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cij ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0G4DBU7_9ACTN A0A0G4DBU7_9ACTN] 
<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 7cij" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces sp. 590 KI-2014]]
[[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]]