5bnc: Difference between revisions
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==Structure of heme binding protein MSMEG_6519 from Mycobacterium smegmatis== | ==Structure of heme binding protein MSMEG_6519 from Mycobacterium smegmatis== | ||
<StructureSection load='5bnc' size='340' side='right' caption='[[5bnc]], [[Resolution|resolution]] 2.25Å' scene=''> | <StructureSection load='5bnc' size='340' side='right'caption='[[5bnc]], [[Resolution|resolution]] 2.25Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5bnc]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5bnc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis_MC2_155 Mycolicibacterium smegmatis MC2 155]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BNC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BNC FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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=5bnc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bnc OCA], [https://pdbe.org/5bnc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bnc RCSB], [https://www.ebi.ac.uk/pdbsum/5bnc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bnc ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0R6E4_MYCS2 A0R6E4_MYCS2] | |||
<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: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mycolicibacterium smegmatis MC2 155]] | ||
[[Category: | [[Category: Ahmed FH]] | ||
[[Category: | [[Category: Carr PD]] | ||
[[Category: | [[Category: Jackson CJ]] | ||
Revision as of 09:00, 7 June 2023
Structure of heme binding protein MSMEG_6519 from Mycobacterium smegmatisStructure of heme binding protein MSMEG_6519 from Mycobacterium smegmatis
Structural highlights
FunctionPublication Abstract from PubMedThe deazaflavin cofactor F420 enhances the persistence of mycobacteria during hypoxia, oxidative stress, and antibiotic treatment. However, the identities and functions of the mycobacterial enzymes that utilize F420 under these conditions have yet to be resolved. In this work, we used sequence similarity networks to analyze the distribution of the largest F420-dependent protein family in mycobacteria. We show that these enzymes are part of a larger split beta-barrel enzyme superfamily (flavin/deazaflavin oxidoreductases, FDORs) that include previously characterized pyridoxamine/pyridoxine-5'-phosphate oxidases and heme oxygenases. We show that these proteins variously utilize F420, flavin mononucleotide, flavin adenine dinucleotide, and heme cofactors. Functional annotation using phylogenetic, structural, and spectroscopic methods revealed their involvement in heme degradation, biliverdin reduction, fatty acid modification, and quinone reduction. Four novel crystal structures show that plasticity in substrate binding pockets and modifications to cofactor binding motifs enabled FDORs to carry out a variety of functions. This systematic classification and analysis provides a framework for further functional analysis of the roles of FDORs in mycobacterial pathogenesis and persistence. Sequence-Structure-Function Classification of a Catalytically Diverse Oxidoreductase Superfamily in Mycobacteria.,Ahmed FH, Carr PD, Lee BM, Afriat-Jurnou L, Mohamed AE, Hong NS, Flanagan J, Taylor MC, Greening C, Jackson CJ J Mol Biol. 2015 Oct 3. pii: S0022-2836(15)00544-6. doi:, 10.1016/j.jmb.2015.09.021. PMID:26434506[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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