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| | <StructureSection load='6mgt' size='340' side='right'caption='[[6mgt]], [[Resolution|resolution]] 2.77Å' scene=''> | | <StructureSection load='6mgt' size='340' side='right'caption='[[6mgt]], [[Resolution|resolution]] 2.77Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6mgt]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_fluorescens_liquefaciens"_flugge_1886 "bacillus fluorescens liquefaciens" flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MGT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MGT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6mgt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_fluorescens Pseudomonas fluorescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MGT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MGT FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.77Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nbaD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=294 "Bacillus fluorescens liquefaciens" Flugge 1886])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</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=6mgt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mgt OCA], [http://pdbe.org/6mgt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mgt RCSB], [http://www.ebi.ac.uk/pdbsum/6mgt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mgt 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=6mgt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mgt OCA], [https://pdbe.org/6mgt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mgt RCSB], [https://www.ebi.ac.uk/pdbsum/6mgt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mgt ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q83V25_PSEFL Q83V25_PSEFL] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus fluorescens liquefaciens flugge 1886]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Daivs, I]] | + | [[Category: Pseudomonas fluorescens]] |
| - | [[Category: Liu, A]] | + | [[Category: Daivs I]] |
| - | [[Category: Matsui, T]] | + | [[Category: Liu A]] |
| - | [[Category: Rubalcava, I]] | + | [[Category: Matsui T]] |
| - | [[Category: Yang, Y]] | + | [[Category: Rubalcava I]] |
| - | [[Category: Decarboxylase]]
| + | [[Category: Yang Y]] |
| - | [[Category: Holo structure]]
| + | |
| - | [[Category: Lyase]]
| + | |
| Structural highlights
Function
Q83V25_PSEFL
Publication Abstract from PubMed
alpha-Amino-beta-carboxymuconate-ε-semialdehyde decarboxylase (ACMSD) plays an important role in L-tryptophan degradation via the kynurenine pathway. ACMSD forms a homodimer and is functionally inactive as a monomer because its catalytic assembly requires an arginine residue from a neighboring subunit. However, how the oligomeric state and self-association of ACMSD are controlled in solution remains unexplored. Here, we demonstrate that ACMSD from Pseudomonas fluorescens can self-assemble into homodimer, tetramer, and higher-order structures. Using size-exclusion chromatography coupled with small-angle X-ray scattering (SEC-SAXS) analysis, we investigated the ACMSD tetramer structure, and fitting the SAXS data with X-ray crystal structures of the monomeric component; we could generate a pseudo-atomic structure of the tetramer. This analysis revealed a tetramer model of ACMSD as a head-on dimer of dimers. We observed that the tetramer is catalytically more active than the dimer and is in equilibrium with the monomer and dimer. Substituting a critical residue of the dimer-dimer interface, His-110, altered the tetramer dissociation profile by increasing the higher-order oligomer portion in solution without changing the X-ray crystal structure. ACMSD self-association was affected by pH, ionic strength, and other electrostatic interactions. Alignment of ACMSD sequences revealed that His-110 is highly conserved in a few bacteria that utilize nitrobenzoic acid as a sole source of carbon and energy, suggesting a dedicated functional role of ACMSD's self-assembly into the tetrameric and higher-order structures. These results indicate that the dynamic oligomerization status potentially regulates ACMSD activity and that SEC-SAXS coupled with X-ray crystallography is a powerful tool for studying protein self-association.
Quaternary structure of alpha-amino-beta-carboxymuconate-ε-semialdehyde decarboxylase (ACMSD) controls its activity.,Yang Y, Davis I, Matsui T, Rubalcava I, Liu A J Biol Chem. 2019 Jun 12. pii: RA119.009035. doi: 10.1074/jbc.RA119.009035. PMID:31189654[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yang Y, Davis I, Matsui T, Rubalcava I, Liu A. Quaternary structure of alpha-amino-beta-carboxymuconate-ε-semialdehyde decarboxylase (ACMSD) controls its activity. J Biol Chem. 2019 Jun 12. pii: RA119.009035. doi: 10.1074/jbc.RA119.009035. PMID:31189654 doi:http://dx.doi.org/10.1074/jbc.RA119.009035
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