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==Crystal structure of DmoA from Hyphomicrobium sulfonivorans== | ==Crystal structure of DmoA from Hyphomicrobium sulfonivorans== | ||
<StructureSection load='6ak1' size='340' side='right' caption='[[6ak1]], [[Resolution|resolution]] 2.28Å' scene=''> | <StructureSection load='6ak1' size='340' side='right'caption='[[6ak1]], [[Resolution|resolution]] 2.28Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6ak1]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AK1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AK1 FirstGlance]. <br> | <table><tr><td colspan='2'>[[6ak1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_baa-113 Atcc baa-113]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AK1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AK1 FirstGlance]. <br> | ||
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dimethyl-sulfide_monooxygenase Dimethyl-sulfide monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.131 1.14.13.131] </span></td></tr> | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dmoA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=121290 ATCC BAA-113])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dimethyl-sulfide_monooxygenase Dimethyl-sulfide monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.131 1.14.13.131] </span></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=6ak1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ak1 OCA], [http://pdbe.org/6ak1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ak1 RCSB], [http://www.ebi.ac.uk/pdbsum/6ak1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ak1 ProSAT]</span></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=6ak1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ak1 OCA], [http://pdbe.org/6ak1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ak1 RCSB], [http://www.ebi.ac.uk/pdbsum/6ak1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ak1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
DmoA is a monooxygenase which uses dioxygen (O2) and reduced flavin mononucleotide (FMNH2) to catalyze the oxidation of dimethylsulfide (DMS). Although it has been characterized, the structure of DmoA remains unknown. Here, the crystal structure of DmoA was determined to a resolution of 2.28 A and was compared with those of its homologues LadA and BdsA. The results showed that their overall structures are similar: they all share a conserved TIM-barrel fold which is composed of eight alpha-helices and eight beta-strands. In addition, they all have five additional insertions. Detailed comparison showed that the structures have notable differences despite their high sequence similarity. The substrate-binding pocket of DmoA is smaller compared with those of LadA and BdsA. | |||
Crystal structure of the dimethylsulfide monooxygenase DmoA from Hyphomicrobium sulfonivorans.,Cao HY, Wang P, Peng M, Shao X, Chen XL, Li CY Acta Crystallogr F Struct Biol Commun. 2018 Dec 1;74(Pt 12):781-786. doi:, 10.1107/S2053230X18015844. Epub 2018 Nov 26. PMID:30511672<ref>PMID:30511672</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6ak1" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Monooxygenase 3D structures|Monooxygenase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Atcc baa-113]] | |||
[[Category: Dimethyl-sulfide monooxygenase]] | [[Category: Dimethyl-sulfide monooxygenase]] | ||
[[Category: Large Structures]] | |||
[[Category: Cao, H Y]] | [[Category: Cao, H Y]] | ||
[[Category: Li, C Y]] | [[Category: Li, C Y]] | ||
Revision as of 12:16, 18 December 2019
Crystal structure of DmoA from Hyphomicrobium sulfonivoransCrystal structure of DmoA from Hyphomicrobium sulfonivorans
Structural highlights
Publication Abstract from PubMedDmoA is a monooxygenase which uses dioxygen (O2) and reduced flavin mononucleotide (FMNH2) to catalyze the oxidation of dimethylsulfide (DMS). Although it has been characterized, the structure of DmoA remains unknown. Here, the crystal structure of DmoA was determined to a resolution of 2.28 A and was compared with those of its homologues LadA and BdsA. The results showed that their overall structures are similar: they all share a conserved TIM-barrel fold which is composed of eight alpha-helices and eight beta-strands. In addition, they all have five additional insertions. Detailed comparison showed that the structures have notable differences despite their high sequence similarity. The substrate-binding pocket of DmoA is smaller compared with those of LadA and BdsA. Crystal structure of the dimethylsulfide monooxygenase DmoA from Hyphomicrobium sulfonivorans.,Cao HY, Wang P, Peng M, Shao X, Chen XL, Li CY Acta Crystallogr F Struct Biol Commun. 2018 Dec 1;74(Pt 12):781-786. doi:, 10.1107/S2053230X18015844. Epub 2018 Nov 26. PMID:30511672[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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