This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1hbz
From Proteopedia
(Difference between revisions)
| (21 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:1hbz.gif|left|200px]]<br /> | ||
| - | <applet load="1hbz" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1hbz, resolution 1.50Å" /> | ||
| - | '''CATALASE FROM MICROCOCCUS LYSODEIKTICU'''<br /> | ||
| - | == | + | ==Catalase from Micrococcus lysodeikticu== |
| - | The three-dimensional crystal structure of catalase from Micrococcus | + | <StructureSection load='1hbz' size='340' side='right'caption='[[1hbz]], [[Resolution|resolution]] 1.50Å' scene=''> |
| + | == 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> | |
| - | + | ||
| - | + | 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]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Micrococcus luteus]] | ||
| + | [[Category: Barynin VV]] | ||
| + | [[Category: Braningen J]] | ||
| + | [[Category: Dauter Z]] | ||
| + | [[Category: Grebenko AI]] | ||
| + | [[Category: Melik-Adamyan WR]] | ||
| + | [[Category: Murshudov GN]] | ||
| + | [[Category: Wilson KS]] | ||
Current revision
Catalase from Micrococcus lysodeikticu
| |||||||||||
