|
|
| Line 3: |
Line 3: |
| | <StructureSection load='1hzu' size='340' side='right'caption='[[1hzu]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='1hzu' size='340' side='right'caption='[[1hzu]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1hzu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HZU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HZU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1hzu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HZU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HZU FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DHE:HEME+D'>DHE</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NIRS ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DHE:HEME+D'>DHE</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Nitrite_reductase_(NO-forming) Nitrite reductase (NO-forming)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.2.1 1.7.2.1] </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=1hzu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hzu OCA], [https://pdbe.org/1hzu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hzu RCSB], [https://www.ebi.ac.uk/pdbsum/1hzu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hzu 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=1hzu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hzu OCA], [https://pdbe.org/1hzu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hzu RCSB], [https://www.ebi.ac.uk/pdbsum/1hzu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hzu ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/NIRS_PSEAE NIRS_PSEAE] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 30: |
Line 31: |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Nitrite reductase 3D structures|Nitrite reductase 3D structures]] | + | *[[Cytochrome c nitrite reductase|Cytochrome c nitrite reductase]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| Line 36: |
Line 37: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Brown, K]] | + | [[Category: Pseudomonas aeruginosa]] |
| - | [[Category: Brunori, M]] | + | [[Category: Brown K]] |
| - | [[Category: Cambillau, C]] | + | [[Category: Brunori M]] |
| - | [[Category: Cutruzzola, F]] | + | [[Category: Cambillau C]] |
| - | [[Category: Tegoni, M]] | + | [[Category: Cutruzzola F]] |
| - | [[Category: Bladed beta propeller]]
| + | [[Category: Tegoni M]] |
| - | [[Category: Cytochrome c]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
NIRS_PSEAE
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 nitrite reductase (NIR) from Pseudomonas aeruginosa (NIR-Pa) is a soluble enzyme catalysing the reduction of nitrite (NO2(-)) to nitric oxide (NO). The enzyme is a 120 kDa homodimer, in which the monomers carry a c-heme domain and a d(1)-heme domain. The structures of the enzyme in both the oxidised and reduced state were solved previously and indicate His327 and His369 as putative catalytic residues. The kinetic characterisation of site-directed mutants has shown that the substitution of either one of these two His with Ala dramatically reduces the physiologically relevant reactivity towards nitrite, leaving the reactivity towards oxygen unaffected. The three-dimensional structures of P. aeruginosa NIR mutant H327A, and H369A in complex with NO have been solved by multiple wavelength anomalous dispersion (MAD), using the iron anomalous signal, and molecular replacement techniques. In both refined crystal structures the c-heme domain, whilst preserving its classical c-type cytochrome fold, has undergone a 60 degrees rigid-body rotation around an axis parallel with the pseudo 8-fold axis of the beta-propeller, and passing through residue Gln115. Even though the distance between the Fe ions of the c and d(1)-heme remains 21 A, the edge-to-edge distance between the two hemes has increased by 5 A. Furthermore the distal side of the d(1)-heme pocket appears to have undergone structural re-arrangement and Tyr10 has moved out of the active site. In the H369A-NO complex, the position and orientation of NO is significantly different from that of the NO bound to the reduced wild-type structure. Our results provide insight into the flexibility of the enzyme and the distinction between nitrite and oxidase reduction mechanisms. Moreover they demonstrate that the two histidine residues play a crucial role in the physiological activity of nitrite reduction, ligand binding and in the structural organisation of nitrite reductase from P. aeruginosa.
Domain swing upon His to Ala mutation in nitrite reductase of Pseudomonas aeruginosa.,Brown K, Roig-Zamboni V, Cutruzzola' F, Arese M, Sun W, Brunori M, Cambillau C, Tegoni M J Mol Biol. 2001 Sep 21;312(3):541-54. PMID:11563915[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Brown K, Roig-Zamboni V, Cutruzzola' F, Arese M, Sun W, Brunori M, Cambillau C, Tegoni M. Domain swing upon His to Ala mutation in nitrite reductase of Pseudomonas aeruginosa. J Mol Biol. 2001 Sep 21;312(3):541-54. PMID:11563915 doi:10.1006/jmbi.2001.4986
|
