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6ohi

From Proteopedia

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Current revision (14:33, 6 March 2024) (edit) (undo)
 
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<StructureSection load='6ohi' size='340' side='right'caption='[[6ohi]], [[Resolution|resolution]] 2.27&Aring;' scene=''>
<StructureSection load='6ohi' size='340' side='right'caption='[[6ohi]], [[Resolution|resolution]] 2.27&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6ohi]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Marm1 Marm1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OHI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OHI FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6ohi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Marinomonas_mediterranea_MMB-1 Marinomonas mediterranea MMB-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OHI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OHI FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.27&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Marme_4087 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=717774 MARM1])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<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=6ohi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ohi OCA], [http://pdbe.org/6ohi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ohi RCSB], [http://www.ebi.ac.uk/pdbsum/6ohi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ohi ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6ohi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ohi OCA], [https://pdbe.org/6ohi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ohi RCSB], [https://www.ebi.ac.uk/pdbsum/6ohi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ohi ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/F2K073_MARM1 F2K073_MARM1]
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Enzymatic dehalogenation is an important and well-studied biological process in both the detoxification and catabolism of small molecules, many of which are anthropogenic in origin. However, dedicated dehalogenation reactions that replace a halogen atom with a hydrogen are rare in the biosynthesis of natural products. In fact, the debrominase Bmp8 is the only known example. It catalyzes the reductive debromination of the coral settlement cue and the potential human toxin 2,3,4,5-tetrabromopyrrole as part of the biosynthesis of the antibiotic pentabromopseudilin. Using a combination of protein crystallography, mutagenesis, and computational modeling, we propose a catalytic mechanism for Bmp8 that is reminiscent of that catalyzed by human deiodinases in the maintenance of thyroid hormones. The identification of the key catalytic residues enabled us to recognize divergent functional homologues of Bmp8. Characterization of one of these homologues demonstrated its debromination activity even though it is found in a completely distinct genomic context. This observation suggests that additional enzymes outside those associated with the tetrabromopyrrole biosynthetic pathway may be able to alter the lifetime of this compound in the environment.
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Bacterial Tetrabromopyrrole Debrominase Shares a Reductive Dehalogenation Strategy with Human Thyroid Deiodinase.,Chekan JR, Lee GY, El Gamal A, Purdy TN, Houk KN, Moore BS Biochemistry. 2019 May 22. doi: 10.1021/acs.biochem.9b00318. PMID:31117392<ref>PMID:31117392</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6ohi" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Marm1]]
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[[Category: Marinomonas mediterranea MMB-1]]
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[[Category: Chekan, J R]]
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[[Category: Chekan JR]]
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[[Category: Moore, B S]]
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[[Category: Moore BS]]
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[[Category: Biosynthetic protein]]
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[[Category: Debrominase]]
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Current revision

Crystal Structure of the Debrominase Bmp8 (Apo)

PDB ID 6ohi

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