6lkp: Difference between revisions

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'''Unreleased structure'''


The entry 6lkp is ON HOLD  until Paper Publication
==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]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6lkp]] is a 6 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6LKP FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6lkp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lkp OCA], [http://pdbe.org/6lkp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6lkp RCSB], [http://www.ebi.ac.uk/pdbsum/6lkp PDBsum], [http://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.


Authors: Minato, T., Teramoto, T., Kakuta, Y., Ogo, S., Yoon, K.S.
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>


Description: Crystal structure of Dps1 from the thermophilic non-heterocystous filamentous cyanobacterium Thermoleptolyngbya sp. O-77
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 6lkp" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Leptolyngbya sp. o-77]]
[[Category: Kakuta, Y]]
[[Category: Minato, T]]
[[Category: Ogo, S]]
[[Category: Ogo, S]]
[[Category: Yoon, K.S]]
[[Category: Minato, T]]
[[Category: Kakuta, Y]]
[[Category: Teramoto, T]]
[[Category: Teramoto, T]]
[[Category: Yoon, K S]]
[[Category: Dna binding protein]]
[[Category: Dodecamer]]
[[Category: Dp]]
[[Category: Ferritin superfamily]]
[[Category: The dna-binding protein from starved cell]]

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