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[[Image:2xvh.jpg|left|200px]]


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==Crystal structure of bacterial flavin containing monooxygenase in complex with NADP==
The line below this paragraph, containing "STRUCTURE_2xvh", creates the "Structure Box" on the page.
<StructureSection load='2xvh' size='340' side='right'caption='[[2xvh]], [[Resolution|resolution]] 2.54&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2xvh]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylophaga_aminisulfidivorans Methylophaga aminisulfidivorans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XVH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XVH FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.54&#8491;</td></tr>
-->
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
{{STRUCTURE_2xvh|  PDB=2xvh  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2xvh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xvh OCA], [https://pdbe.org/2xvh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xvh RCSB], [https://www.ebi.ac.uk/pdbsum/2xvh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xvh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q83XK4_9GAMM Q83XK4_9GAMM]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A bacterial flavin-containing monooxygenase (bFMO) catalyses the oxygenation of indole to produce indigoid compounds. In the reductive half of the indole oxygenation reaction, NADPH acts as a reducing agent, and NADP(+) remains at the active site, protecting bFMO from reoxidation. Here, the crystal structures of bFMO and bFMO in complex with NADP(+), and a mutant bFMO(Y207S), which lacks indole oxygenation activity, with and without indole are reported. The crystal structures revealed overlapping binding sites for NADP(+) and indole, suggestive of a double-displacement reaction mechanism for bFMO. In biochemical assays, indole inhibited NADPH oxidase activity, and NADPH in turn inhibited the binding of indole and decreased indoxyl production. Comparison of the structures of bFMO with and without bound NADP(+) revealed that NADPH induces conformational changes in two active site motifs. One of the motifs contained Arg-229, which participates in interactions with the phosphate group of NADPH and appears be a determinant of the preferential binding of bFMO to NADPH rather than NADH. The second motif contained Tyr-207. The mutant bFMO(Y207S) exhibited very little indoxyl producing activity; however, the NADPH oxidase activity of the mutant was higher than the wild-type enzyme. It suggests a role for Y207, in the protection of hydroperoxyFAD. We describe an indole oxygenation reaction mechanism for bFMO that involves a ping-pong-like interaction of NADPH and indole.


===CRYSTAL STRUCTURE OF BACTERIAL FLAVIN CONTAINING MONOOXYGENASE IN COMPLEX WITH NADP===
Structural and functional analysis of bacterial flavin-containing monooxygenase reveals its ping-pong-type reaction mechanism.,Cho HJ, Cho HY, Kim KJ, Kim MH, Kim SW, Kang BS J Struct Biol. 2011 Jul;175(1):39-48. Epub 2011 Apr 20. PMID:21527346<ref>PMID:21527346</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2xvh" style="background-color:#fffaf0;"></div>


==About this Structure==
==See Also==
[[2xvh]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Methylophaga_aminisulfidivorans Methylophaga aminisulfidivorans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XVH OCA].
*[[Monooxygenase 3D structures|Monooxygenase 3D structures]]
[[Category: Flavin-containing monooxygenase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Methylophaga aminisulfidivorans]]
[[Category: Methylophaga aminisulfidivorans]]
[[Category: Cho, H J.]]
[[Category: Cho HJ]]
[[Category: Kang, B S.]]
[[Category: Kang BS]]

Latest revision as of 16:59, 1 February 2024

Crystal structure of bacterial flavin containing monooxygenase in complex with NADPCrystal structure of bacterial flavin containing monooxygenase in complex with NADP

Structural highlights

2xvh is a 3 chain structure with sequence from Methylophaga aminisulfidivorans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.54Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q83XK4_9GAMM

Publication Abstract from PubMed

A bacterial flavin-containing monooxygenase (bFMO) catalyses the oxygenation of indole to produce indigoid compounds. In the reductive half of the indole oxygenation reaction, NADPH acts as a reducing agent, and NADP(+) remains at the active site, protecting bFMO from reoxidation. Here, the crystal structures of bFMO and bFMO in complex with NADP(+), and a mutant bFMO(Y207S), which lacks indole oxygenation activity, with and without indole are reported. The crystal structures revealed overlapping binding sites for NADP(+) and indole, suggestive of a double-displacement reaction mechanism for bFMO. In biochemical assays, indole inhibited NADPH oxidase activity, and NADPH in turn inhibited the binding of indole and decreased indoxyl production. Comparison of the structures of bFMO with and without bound NADP(+) revealed that NADPH induces conformational changes in two active site motifs. One of the motifs contained Arg-229, which participates in interactions with the phosphate group of NADPH and appears be a determinant of the preferential binding of bFMO to NADPH rather than NADH. The second motif contained Tyr-207. The mutant bFMO(Y207S) exhibited very little indoxyl producing activity; however, the NADPH oxidase activity of the mutant was higher than the wild-type enzyme. It suggests a role for Y207, in the protection of hydroperoxyFAD. We describe an indole oxygenation reaction mechanism for bFMO that involves a ping-pong-like interaction of NADPH and indole.

Structural and functional analysis of bacterial flavin-containing monooxygenase reveals its ping-pong-type reaction mechanism.,Cho HJ, Cho HY, Kim KJ, Kim MH, Kim SW, Kang BS J Struct Biol. 2011 Jul;175(1):39-48. Epub 2011 Apr 20. PMID:21527346[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Cho HJ, Cho HY, Kim KJ, Kim MH, Kim SW, Kang BS. Structural and functional analysis of bacterial flavin-containing monooxygenase reveals its ping-pong-type reaction mechanism. J Struct Biol. 2011 Jul;175(1):39-48. Epub 2011 Apr 20. PMID:21527346 doi:10.1016/j.jsb.2011.04.007

2xvh, resolution 2.54Å

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