4y9i: Difference between revisions

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-'''Unreleased structure'''
+==Structure of F420-H2 Dependent Reductase (FDR-A) msmeg_2027==
+<StructureSection load='4y9i' size='340' side='right' caption='[[4y9i]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4y9i]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y9I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Y9I FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=4y9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y9i OCA], [http://pdbe.org/4y9i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4y9i RCSB], [http://www.ebi.ac.uk/pdbsum/4y9i PDBsum]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The 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.
-The entry 4y9i is ON HOLD  until Paper Publication
+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<ref>PMID:26434506</ref>
-Authors: Ahmed, F.H., Carr, P.D., Jackson, C.J.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description: Structure of F420-H2 Dependent Reductase (FDR-A) msmeg_2027
+<div class="pdbe-citations 4y9i" style="background-color:#fffaf0;"></div>
-[[Category: Unreleased Structures]]
+== References ==
-[[Category: Ahmed, F.H]]
+<references/>
-[[Category: Jackson, C.J]]
+__TOC__
-[[Category: Carr, P.D]]
+</StructureSection>
+[[Category: Ahmed, F H]]
+[[Category: Carr, P D]]
+[[Category: Jackson, C J]]
+[[Category: F420]]
+[[Category: Oxidoreductase]]
+[[Category: Quinone]]
+[[Category: Reductase]]