4lhp: Difference between revisions
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==Crystal Structure of Native FG41Malonate Semialdehyde Decarboxylase== | |||
=== | <StructureSection load='4lhp' size='340' side='right' caption='[[4lhp]], [[Resolution|resolution]] 2.02Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4lhp]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Coryneform_bacterium Coryneform bacterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LHP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LHP FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4lhp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lhp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lhp RCSB], [http://www.ebi.ac.uk/pdbsum/4lhp PDBsum]</span></td></tr> | |||
</table> | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Coryneform bacterium]] | [[Category: Coryneform bacterium]] | ||
[[Category: Guo, Y | [[Category: Guo, Y]] | ||
[[Category: Hackert, M L | [[Category: Hackert, M L]] | ||
[[Category: Johnson, W H | [[Category: Johnson, W H]] | ||
[[Category: Poelarends, G J | [[Category: Poelarends, G J]] | ||
[[Category: Serrano, H | [[Category: Serrano, H]] | ||
[[Category: Whitman, C P | [[Category: Whitman, C P]] | ||
[[Category: Beta-alpha-beta-motif]] | [[Category: Beta-alpha-beta-motif]] | ||
[[Category: Isomerase]] | [[Category: Isomerase]] | ||
[[Category: The tautomerase superfamily]] | [[Category: The tautomerase superfamily]] | ||
