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| | <StructureSection load='1i7p' size='340' side='right'caption='[[1i7p]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='1i7p' size='340' side='right'caption='[[1i7p]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1i7p]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I7P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I7P FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1i7p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I7P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I7P 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></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]] 2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ndh|1ndh]], [[1ib0|1ib0]]</div></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></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cytochrome-b5_reductase Cytochrome-b5 reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.2.2 1.6.2.2] </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=1i7p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i7p OCA], [https://pdbe.org/1i7p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i7p RCSB], [https://www.ebi.ac.uk/pdbsum/1i7p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i7p 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=1i7p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i7p OCA], [https://pdbe.org/1i7p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i7p RCSB], [https://www.ebi.ac.uk/pdbsum/1i7p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i7p ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/NB5R3_RAT NB5R3_RAT]] Desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction.
| + | [https://www.uniprot.org/uniprot/NB5R3_RAT NB5R3_RAT] Desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cytochrome-b5 reductase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Barber, M J]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Bewley, M C]] | + | [[Category: Barber MJ]] |
| - | [[Category: Marohnic, C C]] | + | [[Category: Bewley MC]] |
| - | [[Category: Electron transport]] | + | [[Category: Marohnic CC]] |
| - | [[Category: Erythrocyte function]]
| + | |
| - | [[Category: Fad-binding]]
| + | |
| - | [[Category: Hemoglobinemia]]
| + | |
| - | [[Category: Nadh-binding]]
| + | |
| - | [[Category: Oxygen storage-transport complex]]
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| Structural highlights
Function
NB5R3_RAT Desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction.
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
Cytochrome b5 reductase (cb5r) (EC 1.6.6.2) catalyzes the reduction of two molecules of cytochrome b5 using NADH as the physiological electron donor. The structure of pig cb5r at 2.4 A resolution was previously reported in the literature, but it was inconsistent with the biochemistry; for example, K83 and C245 were both implicated in the mechanism, but were not located at the active site. To address this problem, we have determined the structures of cb5r from rat at 2.0 A resolution and in a complex with NAD+ at 2.3 A resolution. We found significant differences throughout the rat structure compared to that of pig, including the locations of the lysine and cysteine residues mentioned above. To test the structural models, we made single amino acid substitutions of this lysine and showed that all substitutions produced correctly folded proteins and exhibited normal flavin behavior. However, the apparent kcat(NADH) decreased, and the apparent K(m) for NADH increased; the K(m)'s for cytochrome b5 were unchanged relative to that of the wild type. The largest effect was for the glutamate-substituted protein, which was further characterized using a charge transfer assay and found to be less efficient at NADH utilization than the wild type. These results are consistent with a role for this lysine in stabilizing the NADH-bound form of cb5r. We have concluded that the pig structure was mistraced in several regions and have reinterpreted mutants in these regions that give rise to the hereditary disease methemoglobinemia.
The structure and biochemistry of NADH-dependent cytochrome b5 reductase are now consistent.,Bewley MC, Marohnic CC, Barber MJ Biochemistry. 2001 Nov 13;40(45):13574-82. PMID:11695905[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bewley MC, Marohnic CC, Barber MJ. The structure and biochemistry of NADH-dependent cytochrome b5 reductase are now consistent. Biochemistry. 2001 Nov 13;40(45):13574-82. PMID:11695905
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