|
|
| Line 3: |
Line 3: |
| | <StructureSection load='1sy7' size='340' side='right'caption='[[1sy7]], [[Resolution|resolution]] 1.75Å' scene=''> | | <StructureSection load='1sy7' size='340' side='right'caption='[[1sy7]], [[Resolution|resolution]] 1.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1sy7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chrysonilia_crassa Chrysonilia crassa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SY7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SY7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1sy7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Neurospora_crassa Neurospora crassa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SY7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SY7 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HDD:CIS-HEME+D+HYDROXYCHLORIN+GAMMA-SPIROLACTONE'>HDD</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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]] 1.75Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1gge|1gge]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HDD:CIS-HEME+D+HYDROXYCHLORIN+GAMMA-SPIROLACTONE'>HDD</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Catalase Catalase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.6 1.11.1.6] </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=1sy7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sy7 OCA], [https://pdbe.org/1sy7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sy7 RCSB], [https://www.ebi.ac.uk/pdbsum/1sy7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sy7 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=1sy7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sy7 OCA], [https://pdbe.org/1sy7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sy7 RCSB], [https://www.ebi.ac.uk/pdbsum/1sy7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sy7 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/CAT1_NEUCR CAT1_NEUCR]] Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide (By similarity).
| + | [https://www.uniprot.org/uniprot/CAT1_NEUCR CAT1_NEUCR] Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 37: |
Line 36: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Catalase]] | |
| - | [[Category: Chrysonilia crassa]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Arreola, R]] | |
| - | [[Category: Diaz, A]] | |
| - | [[Category: Hansberg, W]] | |
| - | [[Category: Horjales, E]] | |
| - | [[Category: Rudino-Pinera, E]] | |
| - | [[Category: Heme oxidation]] | |
| | [[Category: Neurospora crassa]] | | [[Category: Neurospora crassa]] |
| - | [[Category: Oxidoreductase]] | + | [[Category: Arreola R]] |
| - | [[Category: Singlet oxygen]] | + | [[Category: Diaz A]] |
| | + | [[Category: Hansberg W]] |
| | + | [[Category: Horjales E]] |
| | + | [[Category: Rudino-Pinera E]] |
| Structural highlights
Function
CAT1_NEUCR Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide (By similarity).
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
Catalase-1, one of four catalase activities of Neurospora crassa, is associated with non-growing cells and accumulates in asexual spores. It is a large, tetrameric, highly efficient, and durable enzyme that is active even at molar concentrations of hydrogen peroxide. Catalase-1 is oxidized at the heme by singlet oxygen without significant effects on enzyme activity. Here we present the crystal structure of catalase-1 at 1.75A resolution. Compared to structures of other catalases of the large class, the main differences were found at the carboxy-terminal domain. The heme group is rotated 180 degrees around the alpha-gamma-meso carbon axis with respect to clade 3 small catalases. There is no co-ordination bond of the ferric ion at the heme distal side in catalase-1. The catalase-1 structure exhibited partial oxidation of heme b to heme d. Singlet oxygen, produced catalytically or by photosensitization, may hydroxylate C5 and C6 of pyrrole ring III with a subsequent formation of a gamma-spirolactone in C6. The modification site in catalases depends on the way dioxygen exits the protein: mainly through the central channel or the main channel in large and small catalases, respectively. The catalase-1 structure revealed an unusual covalent bond between a cysteine sulphur atom and the essential tyrosine residue of the proximal side of the active site. A peptide with the predicted theoretical mass of the two bound tryptic peptides was detected by mass spectrometry. A mechanism for the Cys-Tyr covalent bond formation is proposed. The tyrosine bound to the cysteine residue would be less prone to donate electrons to compound I to form compound II, explaining catalase-1 resistance to substrate inhibition and inactivation. An apparent constriction of the main channel at Ser198 lead us to propose a gate that opens the narrow part of the channel when there is sufficient hydrogen peroxide in the small cavity before the gate. This mechanism would explain the increase in catalytic velocity as the hydrogen peroxide concentration rises.
Unusual Cys-Tyr covalent bond in a large catalase.,Diaz A, Horjales E, Rudino-Pinera E, Arreola R, Hansberg W J Mol Biol. 2004 Sep 17;342(3):971-85. PMID:15342250[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Diaz A, Horjales E, Rudino-Pinera E, Arreola R, Hansberg W. Unusual Cys-Tyr covalent bond in a large catalase. J Mol Biol. 2004 Sep 17;342(3):971-85. PMID:15342250 doi:10.1016/j.jmb.2004.07.027
|
