View source for 2yjj


==Structure of Dps from MICROBACTERIUM ARBORESCENS in the low iron form==
<StructureSection load='2yjj' size='340' side='right'caption='[[2yjj]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2yjj]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Microbacterium_arborescens Microbacterium arborescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YJJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YJJ 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]] 2.05&#8491;</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=OFE:IRON(II)+OXIDE'>OFE</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=2yjj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yjj OCA], [https://pdbe.org/2yjj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yjj RCSB], [https://www.ebi.ac.uk/pdbsum/2yjj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yjj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q1X6M4_9MICO Q1X6M4_9MICO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Dps (DNA protection during starvation) enzymes are a major class of dodecameric proteins that bacteria use to detoxify their cytosol through the uptake of reactive iron species. In the stationary growth phase of bacteria, Dps enzymes are primarily used to protect DNA by biocrystallization. To characterize the wild type Dps protein from Microbacterium arborescens that displays additional catalytic functions (amide hydrolysis and synthesis), we determined the crystal structure to a resolution of 2.05 A at low iron content. The structure shows a single iron at the ferroxidase center coordinated by an oxo atom, one water molecule, and three ligating residues. An iron-enriched protein structure was obtained at 2 A and shows the stepwise uptake of two hexahydrated iron atoms moving along channels at the 3-fold axis before a restriction site inside the channels requires removal of the hydration sphere. Supporting biochemical data provide insight into the regulation of this acylamino acid hydrolase. Moreover, the peroxidase activity of the protein was determined. The influence of iron and siderophores on the expression of acylamino acid hydrolase was monitored during several stages of cell growth. Altogether our data provide an interesting view of an unusual Dps-like enzyme evolutionarily located apart from the large Dps sequence clusters.

Structure and Mechanism of Iron Translocation by a Dps Protein from Microbacterium arborescens.,Pesek J, Buchler R, Albrecht R, Boland W, Zeth K J Biol Chem. 2011 Oct 7;286(40):34872-82. Epub 2011 Jul 16. PMID:21768097<ref>PMID:21768097</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2yjj" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Microbacterium arborescens]]
[[Category: Boland W]]
[[Category: Buecheler R]]
[[Category: Zeth K]]