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<StructureSection load='6ihk' size='340' side='right'caption='[[6ihk]], [[Resolution|resolution]] 2.23&Aring;' scene=''>
<StructureSection load='6ihk' size='340' side='right'caption='[[6ihk]], [[Resolution|resolution]] 2.23&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6ihk]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IHK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6IHK FirstGlance]. <br>
<table><tr><td colspan='2'>[[6ihk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ruegeria_lacuscaerulensis_ITI-1157 Ruegeria lacuscaerulensis ITI-1157]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IHK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IHK FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.23&#8491;</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=6ihk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ihk OCA], [http://pdbe.org/6ihk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ihk RCSB], [http://www.ebi.ac.uk/pdbsum/6ihk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ihk ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</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=6ihk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ihk OCA], [https://pdbe.org/6ihk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ihk RCSB], [https://www.ebi.ac.uk/pdbsum/6ihk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ihk ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The vast majority of oceanic dimethylsulfoniopropionate (DMSP) is thought to be catabolized by bacteria via the DMSP demethylation pathway. This pathway contains four enzymes termed DmdA, DmdB, DmdC and DmdD/AcuH, which together catabolize DMSP to acetylaldehyde and methanethiol as carbon and sulfur sources respectively. While molecular mechanisms for DmdA and DmdD have been proposed, little is known of the catalytic mechanisms of DmdB and DmdC, which are central to this pathway. Here, we undertake physiological, structural and biochemical analyses to elucidate the catalytic mechanisms of DmdB and DmdC. DmdB, a 3-methylmercaptopropionate (MMPA)-coenzyme A (CoA) ligase, undergoes two sequential conformational changes to catalyze the ligation of MMPA and CoA. DmdC, a MMPA-CoA dehydrogenase, catalyzes the dehydrogenation of MMPA-CoA to generate MTA-CoA with Glu435 as the catalytic base. Sequence alignment suggests that the proposed catalytic mechanisms of DmdB and DmdC are likely widely adopted by bacteria using the DMSP demethylation pathway. Analysis of the substrate affinities of involved enzymes indicates that Roseobacters kinetically regulate the DMSP demethylation pathway to ensure DMSP functioning and catabolism in their cells. Altogether, this study sheds novel lights on the catalytic and regulative mechanisms of bacterial DMSP demethylation, leading to a better understanding of bacterial DMSP catabolism.
Mechanistic insight into 3-methylmercaptopropionate metabolism and kinetical regulation of demethylation pathway in marine dimethylsulfoniopropionate-catabolizing bacteria.,Shao X, Cao HY, Zhao F, Peng M, Wang P, Li CY, Shi WL, Wei TD, Yuan Z, Zhang XH, Chen XL, Todd JD, Zhang YZ Mol Microbiol. 2019 Apr;111(4):1057-1073. doi: 10.1111/mmi.14211. Epub 2019 Mar, 4. PMID:30677184<ref>PMID:30677184</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6ihk" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Cao, H Y]]
[[Category: Ruegeria lacuscaerulensis ITI-1157]]
[[Category: Chen, X L]]
[[Category: Cao HY]]
[[Category: Li, C Y]]
[[Category: Chen XL]]
[[Category: Peng, M]]
[[Category: Li CY]]
[[Category: Shao, X]]
[[Category: Peng M]]
[[Category: Wang, P]]
[[Category: Shao X]]
[[Category: Zhang, Y Z]]
[[Category: Wang P]]
[[Category: Zhao, F]]
[[Category: Zhang YZ]]
[[Category: Atp dependent]]
[[Category: Zhao F]]
[[Category: Coa ligase]]
[[Category: Dimer]]
[[Category: Ligase]]

Latest revision as of 10:33, 27 March 2024

Structure of MMPA CoA ligase in complex with ADP

6ihk, resolution 2.23Å

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