View source for 3vk2


==Crystal Structure of L-Methionine gamma-Lyase from Pseudomonas putida C116H Mutant.==
<StructureSection load='3vk2' size='340' side='right'caption='[[3vk2]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3vk2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VK2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VK2 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]] 2.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3vk2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vk2 OCA], [https://pdbe.org/3vk2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vk2 RCSB], [https://www.ebi.ac.uk/pdbsum/3vk2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vk2 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MEGL_PSEPU MEGL_PSEPU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cys116, Lys240&lt;sup&gt;*&lt;/sup&gt;, and Asp241&lt;sup&gt;*&lt;/sup&gt; (asterisks indicate residues from the second subunit of the active dimer) at the active site of L-methionine gamma-lyase of Pseudomonas putida (MGL_Pp) are highly conserved among heterologous MGLs. In a previous study, we found that substitution of Cys116 for His led to a drastic increase in activity toward L-cysteine and a decrease in that toward L-methionine. In this study, we examined some properties of the C116H mutant by kinetic analysis and 3D structural analysis. We assumed that substitution of Cys116 for His broke the original hydrogen-bond network and that this induced a significant effect of Tyr114 as a general acid catalyst, possibly due to the narrow space in the active site. The C116H mutant acquired a novel beta-elimination activity and lead a drastic conformation change in the histidine residue at position 116 by binding the substrate, suggesting that this His residue affects the reaction specificity of C116H. Furthermore, we suggest that Lys240&lt;sup&gt;*&lt;/sup&gt; is important for substrate recognition and structural stability and that Asp241&lt;sup&gt;*&lt;/sup&gt; is also involved in substrate specificity in the elimination reaction. Based on this, we suggest that the hydrogen-bond network among Cys116, Lys240&lt;sup&gt;*&lt;/sup&gt;, and Asp241&lt;sup&gt;*&lt;/sup&gt; contributes to substrate specificity that is, to L-methionine recognition at the active site in MGL_Pp.

The Role of Amino Acid Residues in the Active Site of &lt;small&gt;L&lt;/small&gt;-Methionine gamma-lyase from &lt;i&gt;Pseudomonas putida&lt;/i&gt;.,Fukumoto M, Kudou D, Murano S, Shiba T, Sato D, Tamura T, Harada S, Inagaki K Biosci Biotechnol Biochem. 2012 Jul 23;76(7):1275-84. Epub 2012 Jul 7. PMID:22785484<ref>PMID:22785484</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3vk2" style="background-color:#fffaf0;"></div>

==See Also==
*[[Methionine gamma-lyase 3D structures|Methionine gamma-lyase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas putida]]
[[Category: Fukumoto M]]
[[Category: Harada S]]
[[Category: Inagaki K]]
[[Category: Kudou D]]
[[Category: Murano S]]
[[Category: Sato D]]
[[Category: Shiba T]]
[[Category: Tamura T]]