View source for 3mjz


==The crystal structure of native FG41 MSAD==
<StructureSection load='3mjz' size='340' side='right'caption='[[3mjz]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3mjz]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Coryneform_bacterium Coryneform bacterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MJZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MJZ 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]] 2.4&#8491;</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=3mjz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mjz OCA], [https://pdbe.org/3mjz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mjz RCSB], [https://www.ebi.ac.uk/pdbsum/3mjz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mjz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/F2Z288_9CORY F2Z288_9CORY] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Malonate semialdehyde decarboxylase from Pseudomonas pavonaceae 170 (designated Pp MSAD) is in a bacterial catabolic pathway for the nematicide 1,3-dichloropropene. MSAD has two known activities: it catalyzes the metal-ion independent decarboxylation of malonate semialdehyde to produce acetaldehyde and carbon dioxide, as well as a low-level hydration of 2-oxo-3-pentynoate to yield acetopyruvate. The latter activity is not known to be biologically relevant. Previous studies identified Pro-1, Asp-37, and a pair of arginines (Arg-73 and Arg-75) as critical residues in these activities. MSAD from Coryneform bacterium strain FG41 (designated FG41 MSAD) shares 38% pairwise sequence identity with the Pseudomonas enzyme including Pro-1 and Asp-37. However, Gln-73 replaces Arg-73, and the second arginine is shifted to Arg-76 by the insertion of a glycine. In order to determine how these changes relate to the activities of FG41 MSAD, the gene was cloned and the enzyme expressed and characterized. The enzyme has a comparable decarboxylase activity, but a significantly reduced hydratase activity. Mutagenesis along with crystal structures of the native enzyme (2.0 A resolution) and the enzyme modified by a 3-oxopropanoate moiety (resulting from the incubation of enzyme and 3-bromopropiolate) (2.2 A resolution) provided a structural basis. The roles of Pro-1 and Asp-37 are likely the same as those proposed for MSAD. However, the side chains of Thr-72, Gln-73, and Tyr-123 replace those of Arg-73 and Arg-75 in the mechanism and play a role in binding and catalysis. The structures also show that Arg-76 is likely too distant to play a direct role in the mechanism. FG41 MSAD is the second functionally annotated homologue in the MSAD family of the tautomerase superfamily and could represent a new subfamily.

Kinetic, Mutational, and Structural Analysis of Malonate Semialdehyde Decarboxylase from Coryneform bacterium strain FG41: Mechanistic Implications for the Decarboxylase and Hydratase Activities.,Guo Y, Serrano H, Poelarends GJ, Johnson WH, Hackert ML, Whitman CP Biochemistry. 2013 Jun 19. PMID:23781927<ref>PMID:23781927</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3mjz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Coryneform bacterium]]
[[Category: Large Structures]]
[[Category: Guo Y]]
[[Category: Hackert ML]]
[[Category: Johnson WHJr]]
[[Category: Poelarends GJ]]
[[Category: Serrano H]]
[[Category: Whitman CP]]