3mlc: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3mlc]] is a 5 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=3MLC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MLC FirstGlance]. <br> | <table><tr><td colspan='2'>[[3mlc]] is a 5 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=3MLC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MLC FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.224Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PR6:3-CHLORO-3-OXOPROPANOIC+ACID'>PR6</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=3mlc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mlc OCA], [https://pdbe.org/3mlc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mlc RCSB], [https://www.ebi.ac.uk/pdbsum/3mlc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mlc ProSAT]</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=3mlc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mlc OCA], [https://pdbe.org/3mlc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mlc RCSB], [https://www.ebi.ac.uk/pdbsum/3mlc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mlc ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/F2Z288_9CORY F2Z288_9CORY] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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[[Category: Coryneform bacterium]] | [[Category: Coryneform bacterium]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Guo | [[Category: Guo Y]] | ||
[[Category: Hackert | [[Category: Hackert ML]] | ||
[[Category: Johnson | [[Category: Johnson Jr WH]] | ||
[[Category: Poelarends | [[Category: Poelarends GJ]] | ||
[[Category: Serrano | [[Category: Serrano H]] | ||
[[Category: Whitman | [[Category: Whitman CP]] | ||
Latest revision as of 11:55, 6 September 2023
Crystal structure of FG41MSAD inactivated by 3-chloropropiolateCrystal structure of FG41MSAD inactivated by 3-chloropropiolate
Structural highlights
FunctionPublication Abstract from PubMedMalonate 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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