|
|
| Line 3: |
Line 3: |
| | <StructureSection load='1rz1' size='340' side='right'caption='[[1rz1]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='1rz1' size='340' side='right'caption='[[1rz1]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1rz1]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/'geobacillus_thermoglucosidans' 'geobacillus thermoglucosidans']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RZ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RZ1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1rz1]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Parageobacillus_thermoglucosidasius Parageobacillus thermoglucosidasius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RZ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RZ1 FirstGlance]. <br> |
| - | </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=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</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]] 2.1Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1rz0|1rz0]]</div></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=1rz1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rz1 OCA], [https://pdbe.org/1rz1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rz1 RCSB], [https://www.ebi.ac.uk/pdbsum/1rz1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rz1 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=1rz1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rz1 OCA], [https://pdbe.org/1rz1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rz1 RCSB], [https://www.ebi.ac.uk/pdbsum/1rz1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rz1 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9LAG2_PARTM Q9LAG2_PARTM] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 35: |
Line 36: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Geobacillus thermoglucosidans]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Berkel, W J.Van]] | + | [[Category: Parageobacillus thermoglucosidasius]] |
| - | [[Category: Heck, A J]] | + | [[Category: Heck AJ]] |
| - | [[Category: Heuvel, R H.Van Den]]
| + | [[Category: Mattevi A]] |
| - | [[Category: Mattevi, A]] | + | [[Category: Rovida S]] |
| - | [[Category: Rovida, S]] | + | [[Category: Van Berkel WJ]] |
| - | [[Category: Walsh, M A]] | + | [[Category: Van Den Heuvel RH]] |
| - | [[Category: Westphal, A H]] | + | [[Category: Walsh MA]] |
| - | [[Category: Flavin]] | + | [[Category: Westphal AH]] |
| - | [[Category: Nad]] | + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
Q9LAG2_PARTM
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 catabolism of toxic phenols in the thermophilic organism Bacillus thermoglucosidasius A7 is initiated by a two-component enzyme system. The smaller flavin reductase PheA2 component catalyzes the NADH-dependent reduction of free FAD according to a ping-pong bisubstrate-biproduct mechanism. The reduced FAD is then used by the larger oxygenase component PheA1 to hydroxylate phenols to the corresponding catechols. We have determined the x-ray structure of PheA2 containing a bound FAD cofactor (2.2 A), which is the first structure of a member of this flavin reductase family. We have also determined the x-ray structure of reduced holo-PheA2 in complex with oxidized NAD (2.1 A). PheA2 is a single domain homodimeric protein with each FAD-containing subunit being organized around a six-stranded beta-sheet and a capping alpha-helix. The tightly bound FAD prosthetic group (K(d) = 10 nm) binds near the dimer interface, and the re face of the FAD isoalloxazine ring is fully exposed to solvent. The addition of NADH to crystalline PheA2 reduced the flavin cofactor, and the NAD product was bound in a wide solvent-accessible groove adopting an unusual folded conformation with ring stacking. This is the first observation of an enzyme that is very likely to react with a folded compact pyridine nucleotide. The PheA2 crystallographic models strongly suggest that reactive exogenous FAD substrate binds in the NADH cleft after release of NAD product. Nanoflow electrospray mass spectrometry data indeed showed that PheA2 is able to bind one FAD cofactor and one FAD substrate. In conclusion, the structural data provide evidence that PheA2 contains a dual binding cleft for NADH and FAD substrate, which alternate during catalysis.
Structural studies on flavin reductase PheA2 reveal binding of NAD in an unusual folded conformation and support novel mechanism of action.,van den Heuvel RH, Westphal AH, Heck AJ, Walsh MA, Rovida S, van Berkel WJ, Mattevi A J Biol Chem. 2004 Mar 26;279(13):12860-7. Epub 2003 Dec 31. PMID:14703520[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ van den Heuvel RH, Westphal AH, Heck AJ, Walsh MA, Rovida S, van Berkel WJ, Mattevi A. Structural studies on flavin reductase PheA2 reveal binding of NAD in an unusual folded conformation and support novel mechanism of action. J Biol Chem. 2004 Mar 26;279(13):12860-7. Epub 2003 Dec 31. PMID:14703520 doi:10.1074/jbc.M313765200
|
