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.

1n1q

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 08:55, 21 April 2021

Crystal structure of a Dps protein from Bacillus brevis

Structural highlights

1n1q is a 4 chain structure with sequence from Atcc 8246. 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

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The crystallization of cellular components represents a unique survival strategy for bacterial cells under stressed conditions. A highly ordered, layered structure is often formed in such a process, which may involve one or more than one type of bio-macromolecules. The main advantage of biocrystallization has been attributed to the fact that it is a physical process and thus is independent of energy consumption. Dps is a protein that crystallizes to form a multi-layered structure in starved cells in order to protect DNA against oxidative damage and other detrimental factors. The multi-layered crystal structure of a Dps protein from Bacillus brevis has been revealed for the first time at atomic resolution in the absence of DNA. Inspection of the structure provides the first direct evidence for the existence of a di-nuclear ferroxidase center, which possesses unique features among all the di-iron proteins identified so far. It constitutes the structural basis for the ferroxidase activity of Dps in the crystalline state as well as in solution. This finding proves that the enzymatic process of detoxification of metal ions, which may cause severe oxidative damage to DNA, is the other important aspect of the defense mechanism performed by Dps. In the multi-layered structure, Dps dodecamers are organized in a highly ordered manner. They adopt the classic form of hexagonal packing in each layer of the structure. Such arrangement results in reinforced structural features that would facilitate the attraction and absorption of metal ions from the environment. The highly ordered layered structure may provide an ideal basis for the accommodation of DNA between the layers so that it can be isolated and protected from harmful factors under stress conditions.

The multi-layered structure of Dps with a novel di-nuclear ferroxidase center.,Ren B, Tibbelin G, Kajino T, Asami O, Ladenstein R J Mol Biol. 2003 Jun 6;329(3):467-77. PMID:12767829^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Ren B, Tibbelin G, Kajino T, Asami O, Ladenstein R. The multi-layered structure of Dps with a novel di-nuclear ferroxidase center. J Mol Biol. 2003 Jun 6;329(3):467-77. PMID:12767829

1 Structural highlights
2 Evolutionary Conservation
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1n1q"

@@ Line 3: / Line 3: @@
 <StructureSection load='1n1q' size='340' side='right'caption='[[1n1q]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1n1q]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_8246 Atcc 8246]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N1Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1N1Q FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1n1q]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_8246 Atcc 8246]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N1Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N1Q FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FEO:MU-OXO-DIIRON'>FEO</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FEO:MU-OXO-DIIRON'>FEO</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=1n1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n1q OCA], [http://pdbe.org/1n1q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1n1q RCSB], [http://www.ebi.ac.uk/pdbsum/1n1q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1n1q ProSAT]</span></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=1n1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n1q OCA], [https://pdbe.org/1n1q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n1q RCSB], [https://www.ebi.ac.uk/pdbsum/1n1q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n1q ProSAT]</span></td></tr>
 </table>
 == Evolutionary Conservation ==

1n1q

From Proteopedia

Revision as of 08:55, 21 April 2021

Crystal structure of a Dps protein from Bacillus brevis

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox