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4cnk
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4cnk is ON HOLD Authors: Molla, G., Nardini, M., Motta, P., D'Arrigo, P., Bolognesi, M., Pollegioni, L. Description: L-Aminoacetone oxidase from St...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==L-Aminoacetone oxidase from Streptococcus oligofermentans belongs to a new 3-domain family of bacterial flavoproteins== | |
| + | <StructureSection load='4cnk' size='340' side='right'caption='[[4cnk]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4cnk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_cristatus Streptococcus cristatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CNK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CNK 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]] 2Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MEU:O-METHYL-GLYCINE'>MEU</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=4cnk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cnk OCA], [https://pdbe.org/4cnk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cnk RCSB], [https://www.ebi.ac.uk/pdbsum/4cnk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cnk ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/B1PUC6_STRCR B1PUC6_STRCR] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The aaoso gene from Streptococcus oligofermentas encodes for a 43 kDa flavoprotein (SoAAO), which was reported to possess a low catalytic activity versus several different L-amino acids: accordingly, it was classified as an L-amino acid oxidase. Subsequently, SoAAO was demonstrated to oxidize aminoacetone (a prooxidant metabolite), with an activity about 25-folds higher than the activity displayed on L-lysine this yielding support to the assumption of aminoacetone as the preferred substrate. In this work we present a characterization of the SoAAO structure-function relationships. SoAAO is a FAD-containing enzyme that does not possess the classical properties of oxidase/dehydrogenase class of flavoproteins (i.e., no flavin semiquinone formation is observed during anaerobic photoreduction as well as no reaction with sulfite) and does not show a true L-amino acid oxidase activity. From a structural point of view, SoAAO belongs to a novel protein family composed of three domains: an alpha/beta domain corresponding to the FAD-binding domain, a beta-domain partially modulating accessibility to the coenzyme, and an additional alpha-domain. Analysis of the reaction products of SoAAO on aminoacetone showed 2,5-dimethylpyrazine as the main product: we propose that condensation of two aminoacetone molecules yields 3,6-dimethyl-2,5-dihydropyrazine that is subsequently oxidized to 2,5-dimethylpyrazine. The ability of SoAAO to bind two molecules of the substrate-analogue O-methylglycine ligand is held to facilitate the condensation reaction. A specialized role for SoAAO in the microbial defence mechanism related to aminoacetone catabolism through a mechanism yielding dimethylpyrazine derivatives instead of methylglyoxal can be proposed. | ||
| - | + | Aminoacetone oxidase from Streptococcus oligofermentas belongs to a new three-domain family of bacterial flavoproteins.,Molla G, Nardini M, Motta P, D'Arrigo P, Panzeri W, Pollegioni L Biochem J. 2014 Sep 30. PMID:25269103<ref>PMID:25269103</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4cnk" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Amino acid oxidase 3D structures|Amino acid oxidase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Streptococcus cristatus]] | ||
| + | [[Category: Bolognesi M]] | ||
| + | [[Category: D'Arrigo P]] | ||
| + | [[Category: Molla G]] | ||
| + | [[Category: Motta P]] | ||
| + | [[Category: Nardini M]] | ||
| + | [[Category: Pollegioni L]] | ||
Current revision
L-Aminoacetone oxidase from Streptococcus oligofermentans belongs to a new 3-domain family of bacterial flavoproteins
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