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==Crystal structure of Dps1 from the thermophilic non-heterocystous filamentous cyanobacterium Thermoleptolyngbya sp. O-77== | |||
<StructureSection load='6lkp' size='340' side='right'caption='[[6lkp]], [[Resolution|resolution]] 2.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6lkp]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Leptolyngbya_sp._O-77 Leptolyngbya sp. O-77]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LKP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LKP 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]] 2.9Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=6lkp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lkp OCA], [https://pdbe.org/6lkp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lkp RCSB], [https://www.ebi.ac.uk/pdbsum/6lkp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lkp ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The DNA-binding protein from starved cells (Dps) is found in a wide range of microorganisms, and it has been well characterized. However, little is known about Dps proteins from non-heterocystous filamentous cyanobacteria. In this study, a Dps protein from the thermophilic non-heterocystous filamentous cyanobacterium Thermoleptolyngbya sp. O-77 (TlDps1) was purified and characterized. PAGE and CD analyses of TlDps1 demonstrated that it had higher thermostability than previously reported Dps proteins. X-ray crystallographic analysis revealed that TlDps1 possessed His-type ferroxidase centers within the cavity and unique metal binding sites located on the surface of the protein, which presumably contributed to its exceedingly high thermostability. | |||
Biochemical and structural characterization of a thermostable Dps protein with His-type ferroxidase centers and outer metal-binding sites.,Minato T, Teramoto T, Kakuta Y, Ogo S, Yoon KS FEBS Open Bio. 2020 Mar 14. doi: 10.1002/2211-5463.12837. PMID:32170832<ref>PMID:32170832</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6lkp" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: Minato | ==See Also== | ||
[[Category: | *[[Ferritin 3D structures|Ferritin 3D structures]] | ||
[[Category: Teramoto | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Leptolyngbya sp. O-77]] | |||
[[Category: Kakuta Y]] | |||
[[Category: Minato T]] | |||
[[Category: Ogo S]] | |||
[[Category: Teramoto T]] | |||
[[Category: Yoon KS]] | |||
Latest revision as of 14:03, 22 November 2023
Crystal structure of Dps1 from the thermophilic non-heterocystous filamentous cyanobacterium Thermoleptolyngbya sp. O-77Crystal structure of Dps1 from the thermophilic non-heterocystous filamentous cyanobacterium Thermoleptolyngbya sp. O-77
Structural highlights
Publication Abstract from PubMedThe DNA-binding protein from starved cells (Dps) is found in a wide range of microorganisms, and it has been well characterized. However, little is known about Dps proteins from non-heterocystous filamentous cyanobacteria. In this study, a Dps protein from the thermophilic non-heterocystous filamentous cyanobacterium Thermoleptolyngbya sp. O-77 (TlDps1) was purified and characterized. PAGE and CD analyses of TlDps1 demonstrated that it had higher thermostability than previously reported Dps proteins. X-ray crystallographic analysis revealed that TlDps1 possessed His-type ferroxidase centers within the cavity and unique metal binding sites located on the surface of the protein, which presumably contributed to its exceedingly high thermostability. Biochemical and structural characterization of a thermostable Dps protein with His-type ferroxidase centers and outer metal-binding sites.,Minato T, Teramoto T, Kakuta Y, Ogo S, Yoon KS FEBS Open Bio. 2020 Mar 14. doi: 10.1002/2211-5463.12837. PMID:32170832[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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