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7xnz
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Native cystathionine beta-synthase of Mycobacterium tuberculosis.== | |
| + | <StructureSection load='7xnz' size='340' side='right'caption='[[7xnz]], [[Resolution|resolution]] 3.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7xnz]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7XNZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XNZ FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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=7xnz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xnz OCA], [https://pdbe.org/7xnz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xnz RCSB], [https://www.ebi.ac.uk/pdbsum/7xnz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xnz ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Y1077_MYCTU Y1077_MYCTU] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Methionine and cysteine metabolisms are important for the survival and pathogenesis of Mycobacterium tuberculosis (Mtb). The transsulfuration pathway converts methionine to cysteine and represents an important link between antioxidant and methylation metabolism in diverse organisms. Using a combination of biochemistry and cryo-electron microscopy, we characterized the first enzyme of the transsulfuration pathway, cystathionine beta-synthase (MtbCbs) in Mtb. We demonstrated that MtbCbs is a heme-less, pyridoxal-5'-phosphate-containing enzyme, allosterically activated by S-adenosylmethionine (SAM). The atomic model of MtbCbs in its native and SAM-bound conformations revealed a unique mode of SAM-dependent allosteric activation. Further, SAM stabilized MtbCbs by sterically occluding proteasomal degradation, which was crucial for supporting methionine and redox metabolism in Mtb. Genetic deficiency of MtbCbs reduced Mtb survival upon homocysteine overload in vitro, inside macrophages, and in mice coinfected with HIV. Thus, the MtbCbs-SAM axis constitutes an important mechanism of coordinating sulfur metabolism in Mtb. | ||
| - | + | S-Adenosylmethionine-responsive cystathionine beta-synthase modulates sulfur metabolism and redox balance in Mycobacterium tuberculosis.,Bandyopadhyay P, Pramanick I, Biswas R, Ps S, Sreedharan S, Singh S, Rajmani RS, Laxman S, Dutta S, Singh A Sci Adv. 2022 Jun 24;8(25):eabo0097. doi: 10.1126/sciadv.abo0097. Epub 2022 Jun , 24. PMID:35749503<ref>PMID:35749503</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 7xnz" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mycobacterium tuberculosis H37Rv]] | ||
| + | [[Category: Bandyopadhyay P]] | ||
| + | [[Category: Biswas R]] | ||
| + | [[Category: Dutta S]] | ||
| + | [[Category: Laxman S]] | ||
| + | [[Category: Pramanick I]] | ||
| + | [[Category: Rajmani R]] | ||
| + | [[Category: Sabarinath PS]] | ||
| + | [[Category: Singh A]] | ||
| + | [[Category: Singh S]] | ||
| + | [[Category: Sreedharan S]] | ||
Current revision
Native cystathionine beta-synthase of Mycobacterium tuberculosis.
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