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1hbz
From Proteopedia
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| - | [[Image:1hbz.jpg|left|200px]] | ||
| - | < | + | ==Catalase from Micrococcus lysodeikticu== |
| - | + | <StructureSection load='1hbz' size='340' side='right'caption='[[1hbz]], [[Resolution|resolution]] 1.50Å' scene=''> | |
| - | You may | + | == Structural highlights == |
| - | + | <table><tr><td colspan='2'>[[1hbz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Micrococcus_luteus Micrococcus luteus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HBZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HBZ FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> | |
| - | -- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1hbz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hbz OCA], [https://pdbe.org/1hbz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hbz RCSB], [https://www.ebi.ac.uk/pdbsum/1hbz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hbz ProSAT]</span></td></tr> | |
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CATA_MICLU CATA_MICLU] Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hb/1hbz_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1hbz ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The three-dimensional crystal structure of catalase from Micrococcus lysodeikticus has been solved by multiple isomorphous replacement and refined at 1.5 A resolution. The subunit of the tetrameric molecule of 222 symmetry consists of a single polypeptide chain of about 500 amino acid residues and one haem group. The crystals belong to space group P4(2)2(1)2 with unit cell parameters a = b = 106.7 A, c = 106.3 A, and there is one subunit of the tetramer per asymmetric unit. The amino acid sequence has been tentatively determined by computer graphics model building and comparison with the known three-dimensional structure of beef liver catalase and sequences of several other catalases. The atomic model has been refined by Hendrickson and Konnert's least-squares minimisation against 94,315 reflections between 8 A and 1.5 A. The final model consists of 3,977 non-hydrogen atoms of the protein and haem group, 426 water molecules and one sulphate ion. The secondary and tertiary structures of the bacterial catalase have been analyzed and a comparison with the structure of beef liver catalase has been made. | ||
| - | + | Three-dimensional structure of catalase from Micrococcus lysodeikticus at 1.5 A resolution.,Murshudov GN, Melik-Adamyan WR, Grebenko AI, Barynin VV, Vagin AA, Vainshtein BK, Dauter Z, Wilson KS FEBS Lett. 1992 Nov 9;312(2-3):127-31. PMID:1426241<ref>PMID:1426241</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 1hbz" style="background-color:#fffaf0;"></div> | ||
| - | == | + | ==See Also== |
| - | + | *[[Catalase 3D structures|Catalase 3D structures]] | |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Micrococcus luteus]] | [[Category: Micrococcus luteus]] | ||
| - | + | [[Category: Barynin VV]] | |
| - | [[Category: Barynin | + | [[Category: Braningen J]] |
| - | [[Category: Braningen | + | [[Category: Dauter Z]] |
| - | [[Category: Dauter | + | [[Category: Grebenko AI]] |
| - | [[Category: Grebenko | + | [[Category: Melik-Adamyan WR]] |
| - | [[Category: Melik-Adamyan | + | [[Category: Murshudov GN]] |
| - | [[Category: Murshudov | + | [[Category: Wilson KS]] |
| - | [[Category: Wilson | + | |
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Current revision
Catalase from Micrococcus lysodeikticu
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