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6dqp

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Crystal structure of SsuE FMN reductase Delta118 mutant in apo form

Structural highlights

6dqp is a 2 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.546Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SSUE_ECOLI Catalyzes an NADPH-dependent reduction of FMN, but is also able to reduce FAD or riboflavin.

Publication Abstract from PubMed

The pi-helix located at the tetramer interface of two-component FMN-dependent reductases contributes to the structural divergence from canonical FMN-bound reductases within the NADPH:FMN reductase family. The pi-helix in the SsuE FMN-dependent reductase of the alkanesulfonate monooxygenase system has been proposed to be generated by the insertion of a Tyr residue in the conserved alpha4-helix. Variants of Tyr118 were generated, and their X-ray crystal structures determined, to evaluate how these alterations affect the structural integrity of the pi-helix. The structure of the Y118A SsuE pi-helix was converted to an alpha-helix, similar to the FMN-bound members of the NADPH:FMN reductase family. Although the pi-helix was altered, the FMN binding region remained unchanged. Conversely, deletion of Tyr118 disrupted the secondary structural properties of the pi-helix, generating a random coil region in the middle of helix 4. Both the Y118A and Delta118 SsuE SsuE variants crystallize as a dimer. The MsuE FMN reductase involved in the desulfonation of methanesulfonates is structurally similar to SsuE, but the pi-helix contains a His insertional residue. Exchanging the pi-helix insertional residue of each enzyme did not result in equivalent kinetic properties. Structure-based sequence analysis further demonstrated the presence of a similar Tyr residue in an FMN-bound reductase in the NADPH:FMN reductase family that is not sufficient to generate a pi-helix. Results from the structural and functional studies of the FMN-dependent reductases suggest that the insertional residue alone is not solely responsible for generating the pi-helix, and additional structural adaptions occur to provide the altered gain of function.

Not as easy as pi: An insertional residue does not explain the pi-helix gain-of-function in two-component FMN reductases.,McFarlane JS, Hagen RA, Chilton AS, Forbes DL, Lamb AL, Ellis HR Protein Sci. 2019 Jan;28(1):123-134. doi: 10.1002/pro.3504. Epub 2018 Nov 15. PMID:30171650^[1]

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

References

↑ McFarlane JS, Hagen RA, Chilton AS, Forbes DL, Lamb AL, Ellis HR. Not as easy as pi: An insertional residue does not explain the pi-helix gain-of-function in two-component FMN reductases. Protein Sci. 2019 Jan;28(1):123-134. doi: 10.1002/pro.3504. Epub 2018 Nov 15. PMID:30171650 doi:http://dx.doi.org/10.1002/pro.3504

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6dqp"

Categories: Escherichia coli K-12 | Large Structures | Ellis HR | Lamb AL | McFarlane JS

@@ Line 1: / Line 1: @@
 ==Crystal structure of SsuE FMN reductase Delta118 mutant in apo form==
-<StructureSection load='6dqp' size='340' side='right' caption='[[6dqp]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
+<StructureSection load='6dqp' size='340' side='right'caption='[[6dqp]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6dqp]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DQP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DQP FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6dqp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DQP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6DQP FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.546&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/FMN_reductase_(NADPH) FMN reductase (NADPH)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.38 1.5.1.38] </span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=6dqp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dqp OCA], [http://pdbe.org/6dqp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dqp RCSB], [http://www.ebi.ac.uk/pdbsum/6dqp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dqp ProSAT]</span></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=6dqp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dqp OCA], [https://pdbe.org/6dqp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6dqp RCSB], [https://www.ebi.ac.uk/pdbsum/6dqp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6dqp ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/SSUE_ECOLI SSUE_ECOLI]] Catalyzes an NADPH-dependent reduction of FMN, but is also able to reduce FAD or riboflavin.
+[https://www.uniprot.org/uniprot/SSUE_ECOLI SSUE_ECOLI] Catalyzes an NADPH-dependent reduction of FMN, but is also able to reduce FAD or riboflavin.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Ellis, H R]]
+[[Category: Escherichia coli K-12]]
-[[Category: Lamb, A L]]
+[[Category: Large Structures]]
-[[Category: McFarlane, J S]]
+[[Category: Ellis HR]]
-[[Category: Flavoprotein]]
+[[Category: Lamb AL]]
-[[Category: Fmn]]
+[[Category: McFarlane JS]]
-[[Category: Oxidoreductase]]
-[[Category: Reductase]]

6dqp

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Current revision

Crystal structure of SsuE FMN reductase Delta118 mutant in apo form

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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