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| | <StructureSection load='1x77' size='340' side='right'caption='[[1x77]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='1x77' size='340' side='right'caption='[[1x77]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1x77]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseae Pseae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X77 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1X77 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1x77]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X77 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1X77 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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]] 2.7Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1rtt|1rtt]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1x77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x77 OCA], [http://pdbe.org/1x77 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1x77 RCSB], [http://www.ebi.ac.uk/pdbsum/1x77 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1x77 ProSAT], [http://www.topsan.org/Proteins/NYSGXRC/1x77 TOPSAN]</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=1x77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x77 OCA], [https://pdbe.org/1x77 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1x77 RCSB], [https://www.ebi.ac.uk/pdbsum/1x77 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1x77 ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/1x77 TOPSAN]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/FMNRE_PSEAE FMNRE_PSEAE] Has NAD(P)H-dependent FMN reductase activity.<ref>PMID:16552139</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pseae]] | + | [[Category: Pseudomonas aeruginosa PAO1]] |
| - | [[Category: Agarwal, R]] | + | [[Category: Agarwal R]] |
| - | [[Category: Burley, S K]] | + | [[Category: Burley SK]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Swaminathan S]] |
| - | [[Category: Swaminathan, S]] | + | |
| - | [[Category: Fmn bound]]
| + | |
| - | [[Category: Fmn reductase]]
| + | |
| - | [[Category: NYSGXRC, New York SGX Research Center for Structural Genomics]]
| + | |
| - | [[Category: Unknown function]]
| + | |
| Structural highlights
Function
FMNRE_PSEAE Has NAD(P)H-dependent FMN reductase activity.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The availability of high-intensity synchrotron facilities, technological advances in data-collection techniques and improved data-reduction and crystallographic software have ushered in a new era in high-throughput macromolecular crystallography. Here, the de novo automated crystal structure determination at 1.28 A resolution of an NAD(P)H-dependent FMN reductase flavoprotein from Pseudomonas aeruginosa PA01-derived protein Q9I4D4 using the anomalous signal from an unusually small number of S atoms is reported. Although this protein lacks the flavodoxin key fingerprint motif [(T/S)XTGXT], it has been confirmed to bind flavin mononucleotide and the binding site was identified via X-ray crystallography. This protein contains a novel flavin mononucleotide-binding site GSLRSGSYN, which has not been previously reported. Detailed statistics pertaining to sulfur phasing and other factors contributing to structure determination are discussed. Structural comparisons of the apoenzyme and the protein complexed with flavin mononucleotide show conformational changes on cofactor binding. NADPH-dependent activity has been confirmed with biochemical assays.
Structure determination of an FMN reductase from Pseudomonas aeruginosa PA01 using sulfur anomalous signal.,Agarwal R, Bonanno JB, Burley SK, Swaminathan S Acta Crystallogr D Biol Crystallogr. 2006 Apr;62(Pt 4):383-91. Epub 2006, Mar 18. PMID:16552139[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Agarwal R, Bonanno JB, Burley SK, Swaminathan S. Structure determination of an FMN reductase from Pseudomonas aeruginosa PA01 using sulfur anomalous signal. Acta Crystallogr D Biol Crystallogr. 2006 Apr;62(Pt 4):383-91. Epub 2006, Mar 18. PMID:16552139 doi:http://dx.doi.org/10.1107/S0907444906001600
- ↑ Agarwal R, Bonanno JB, Burley SK, Swaminathan S. Structure determination of an FMN reductase from Pseudomonas aeruginosa PA01 using sulfur anomalous signal. Acta Crystallogr D Biol Crystallogr. 2006 Apr;62(Pt 4):383-91. Epub 2006, Mar 18. PMID:16552139 doi:http://dx.doi.org/10.1107/S0907444906001600
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