5xe5: Difference between revisions
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<StructureSection load='5xe5' size='340' side='right'caption='[[5xe5]], [[Resolution|resolution]] 2.17Å' scene=''> | <StructureSection load='5xe5' size='340' side='right'caption='[[5xe5]], [[Resolution|resolution]] 2.17Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5xe5]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5xe5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacteroides_abscessus_ATCC_19977 Mycobacteroides abscessus ATCC 19977]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XE5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XE5 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]] 2.17Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5xe5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xe5 OCA], [https://pdbe.org/5xe5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xe5 RCSB], [https://www.ebi.ac.uk/pdbsum/5xe5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xe5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/PHY_MYCA9 PHY_MYCA9] Catalyzes the hydrolytic C-C cleavage of phloretin to phloroglucinol and 3-(4-hydroxyphenyl)propionic acid. Can also hydrolyze monoacetylphloroglucinol (MAPG) but not 2,4-diacetylphloroglucinol (DAPG).<ref>PMID:30784195</ref> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mycobacteroides abscessus ATCC 19977]] | ||
[[Category: Han | [[Category: Han JT]] | ||
[[Category: He | [[Category: He YX]] | ||
[[Category: Jia | [[Category: Jia WJ]] | ||
[[Category: Zhang | [[Category: Zhang Z]] | ||
Latest revision as of 11:00, 22 November 2023
Discovery and structural analysis of a phloretin hydrolase from the opportunistic pathogen Mycobacterium abscessusDiscovery and structural analysis of a phloretin hydrolase from the opportunistic pathogen Mycobacterium abscessus
Structural highlights
FunctionPHY_MYCA9 Catalyzes the hydrolytic C-C cleavage of phloretin to phloroglucinol and 3-(4-hydroxyphenyl)propionic acid. Can also hydrolyze monoacetylphloroglucinol (MAPG) but not 2,4-diacetylphloroglucinol (DAPG).[1] Publication Abstract from PubMedThe family of PhlG proteins catalyses the hydrolysis of carbon-carbon bonds and is widely distributed across diverse bacterial species. Two members of the PhlG family have been separately identified as 2,4-diacetylphloroglucinol (2,4-DAPG) hydrolase and phloretin hydrolase; however, the extent of functional divergence and catalytic substrates for most members of this family is still unknown. Here, using sequence similarity network and gene co-occurrence analysis, we categorized PhlG proteins into several subgroups and inferred that PhlG proteins from Mycobacterium abscessus (MaPhlG) are likely to be functionally equivalent to phloretin hydrolase. Indeed, we confirmed the hydrolytic activity of MaPhlG towards phloretin and its analog monoacetylphloroglucinol (MAPG), and the crystal structure of MaPhlG in complex with MAPG revealed the key residues involved in catalysis and substrate binding. Through mutagenesis and enzymatic assays, we demonstrated that H160, I162, A213 and Q266, which are substituted in 2,4-DAPG hydrolase, are essential for the activity towards phloretin. Based on the conservation of these residues, potential phloretin hydrolases were identified from Frankia, Colletotrichum tofieldiae and Magnaporthe grisea, which are rhizosphere inhabitants. These enzymes may be important for rhizosphere adaptation of the producing microbes by providing a carbon source through anaerobic degradation of flavonoids. Taken together, our results provided a framework for understanding the mechanism of functional divergence of PhlG proteins. Discovery and structural analysis of a phloretin hydrolase from the opportunistic human pathogen Mycobacterium abscessus.,Han JT, Zhang SP, Jia WJ, Zhang Z, Wang Y, He YX FEBS J. 2019 Feb 19. doi: 10.1111/febs.14792. PMID:30784195[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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