6o0a
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
==Crystal structure of flavohemoglobin from Malassezia yamatoensis with bound FAD and heme determined by iron SAD phasing== | ==Crystal structure of flavohemoglobin from Malassezia yamatoensis with bound FAD and heme determined by iron SAD phasing== | ||
| - | <StructureSection load='6o0a' size='340' side='right' | + | <StructureSection load='6o0a' size='340' side='right'caption='[[6o0a]], [[Resolution|resolution]] 1.70Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6o0a]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O0A OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[6o0a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cbs_9725 Cbs 9725]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O0A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6O0A FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr> | + | </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=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</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=6o0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o0a OCA], [https://pdbe.org/6o0a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6o0a RCSB], [https://www.ebi.ac.uk/pdbsum/6o0a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6o0a ProSAT]</span></td></tr> |
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The skin of humans and animals is colonized by commensal and pathogenic fungi and bacteria that share this ecological niche and have established microbial interactions. Malassezia are the most abundant fungal skin inhabitant of warm-blooded animals and have been implicated in skin diseases and systemic disorders, including Crohn's disease and pancreatic cancer. Flavohemoglobin is a key enzyme involved in microbial nitrosative stress resistance and nitric oxide degradation. Comparative genomics and phylogenetic analyses within the Malassezia genus revealed that flavohemoglobin-encoding genes were acquired through independent horizontal gene transfer events from different donor bacteria that are part of the mammalian microbiome. Through targeted gene deletion and functional complementation in Malassezia sympodialis, we demonstrated that bacterially derived flavohemoglobins are cytoplasmic proteins required for nitric oxide detoxification and nitrosative stress resistance under aerobic conditions. RNA-sequencing analysis revealed that endogenous accumulation of nitric oxide resulted in up-regulation of genes involved in stress response and down-regulation of the MalaS7 allergen-encoding genes. Solution of the high-resolution X-ray crystal structure of Malassezia flavohemoglobin revealed features conserved with both bacterial and fungal flavohemoglobins. In vivo pathogenesis is independent of Malassezia flavohemoglobin. Lastly, we identified an additional 30 genus- and species-specific horizontal gene transfer candidates that might have contributed to the evolution of this genus as the most common inhabitants of animal skin. | ||
| + | |||
| + | HGT in the human and skin commensal Malassezia: A bacterially derived flavohemoglobin is required for NO resistance and host interaction.,Ianiri G, Coelho MA, Ruchti F, Sparber F, McMahon TJ, Fu C, Bolejack M, Donovan O, Smutney H, Myler P, Dietrich F, Fox D 3rd, LeibundGut-Landmann S, Heitman J Proc Natl Acad Sci U S A. 2020 Jul 7;117(27):15884-15894. doi:, 10.1073/pnas.2003473117. Epub 2020 Jun 23. PMID:32576698<ref>PMID:32576698</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6o0a" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Cbs 9725]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Structural genomic]] | [[Category: Structural genomic]] | ||
[[Category: Fad]] | [[Category: Fad]] | ||
Revision as of 11:46, 23 March 2022
Crystal structure of flavohemoglobin from Malassezia yamatoensis with bound FAD and heme determined by iron SAD phasing
| |||||||||||
