|
|
| Line 1: |
Line 1: |
| | | | |
| | ==Crystal structure of KatB, a manganese catalase from Anabaena PCC7120== | | ==Crystal structure of KatB, a manganese catalase from Anabaena PCC7120== |
| - | <StructureSection load='4r42' size='340' side='right' caption='[[4r42]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='4r42' size='340' side='right'caption='[[4r42]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4r42]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Anabaena_7120 Anabaena 7120]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R42 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R42 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4r42]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Nostoc_sp._PCC_7120_=_FACHB-418 Nostoc sp. PCC 7120 = FACHB-418]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R42 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R42 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">alr3090 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=103690 Anabaena 7120])</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=4r42 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r42 OCA], [https://pdbe.org/4r42 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r42 RCSB], [https://www.ebi.ac.uk/pdbsum/4r42 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r42 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4r42 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r42 OCA], [http://pdbe.org/4r42 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r42 RCSB], [http://www.ebi.ac.uk/pdbsum/4r42 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4r42 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8YSJ5_NOSS1 Q8YSJ5_NOSS1] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 21: |
Line 22: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Anabaena 7120]] | + | [[Category: Large Structures]] |
| - | [[Category: Bihani, S C]] | + | [[Category: Nostoc sp. PCC 7120 = FACHB-418]] |
| - | [[Category: Helix bundle]] | + | [[Category: Bihani SC]] |
| - | [[Category: Catalase]]
| + | |
| - | [[Category: Manganese]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
4r42 is a 3 chain structure with sequence from Nostoc sp. PCC 7120 = FACHB-418. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
Q8YSJ5_NOSS1
Publication Abstract from PubMed
Manganese catalases (Mn-catalases), a class of H2O2 detoxifying proteins, are structurally and mechanistically distinct from the commonly occurring catalases, which contain heme. Active site of Mn-catalases can serve as template for the synthesis of catalase mimetics for therapeutic intervention in oxidative stress related disorders. However, unlike the heme catalases, structural aspects of Mn-catalases remain inadequately explored. The genome of the ancient cyanobacterium Anabaena PCC7120, shows the presence of two Mn-catalases, KatA and KatB. Here, we report the biochemical and structural characterization of KatB. The KatB protein (with a C-terminal his-tag) was over-expressed in Escherichia coli and purified by affinity chromatography. On the addition of Mn(2+) to the E. coli growth medium, a substantial increase in production of the soluble KatB protein was observed. The purified KatB protein was an efficient catalase, which was relatively insensitive to inhibition by azide. Crystal structure of KatB showed a hexameric assembly with four-helix bundle fold, characteristic of the Ferritin-like superfamily. With canonical Glu4His2 coordination geometry and two terminal water ligands, the KatB active site was distinctly different from that of other Mn-catalases. Interestingly, the KatB active site closely resembled the active sites of ruberythrin/bacterioferritin, bi-iron members of the Ferritin-like superfamily. The KatB crystal structure provided fundamental insights into the evolutionary relationship within the Ferritin-like superfamily and further showed that Mn-catalases can be sub-divided into two groups, each with a distinct active site configuration.
KatB, a cyanobacterial Mn-catalase with unique active site configuration: Implications for enzyme function.,Bihani SC, Chakravarty D, Ballal A Free Radic Biol Med. 2016 Apr;93:118-29. doi:, 10.1016/j.freeradbiomed.2016.01.022. Epub 2016 Jan 27. PMID:26826576[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bihani SC, Chakravarty D, Ballal A. KatB, a cyanobacterial Mn-catalase with unique active site configuration: Implications for enzyme function. Free Radic Biol Med. 2016 Apr;93:118-29. doi:, 10.1016/j.freeradbiomed.2016.01.022. Epub 2016 Jan 27. PMID:26826576 doi:http://dx.doi.org/10.1016/j.freeradbiomed.2016.01.022
|
