7cif: Difference between revisions
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==Crystal structure of L-methionine decarboxylase from Streptomyces sp.590 (internal aldimine form).== | |||
<StructureSection load='7cif' size='340' side='right'caption='[[7cif]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7cif]] 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=7CIF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CIF FirstGlance]. <br> | |||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Lyase Lyase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.57 4.1.1.57] </span></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=7cif FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cif OCA], [https://pdbe.org/7cif PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cif RCSB], [https://www.ebi.ac.uk/pdbsum/7cif PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cif 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7cif" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Lyase]] | |||
[[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: Onoue, Y]] | ||
[[Category: Sato, D]] | [[Category: Sato, D]] | ||
[[Category: Shiba, T]] | [[Category: Shiba, T]] | ||
[[Category: Tamura, T]] | [[Category: Tamura, T]] | ||
[[Category: | [[Category: Decarboxylase]] | ||
[[Category: Plp-dependent enzyme]] | |||