2c41
From Proteopedia
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X-RAY STRUCTURE OF DPS FROM THERMOSYNECHOCOCCUS ELONGATUS
Overview
DNA-binding proteins from starved cells (Dps proteins) protect bacteria, primarily from oxidative damage. They are composed of 12 identical, subunits assembled with 23-symmetry to form a compact cage-like structure, known to be stable at temperatures > 70 degrees C and over a wide pH, range. Thermosynechococcus elongatus Dps thermostability is increased, dramatically relative to mesophilic Dps proteins. Hydrophobic interactions, at the dimeric and trimeric interfaces called Dps-like are replaced by, salt bridges and hydrogen bonds, a common strategy in thermophiles., Moreover, the buried surface area at the least-extended Dps-like interface, is significantly increased. A peculiarity of T. elongatus Dps is the, presence of a chloride ion coordinated with threefold symmetry-related, ... [(full description)]
About this Structure
2C41 is a [Single protein] structure of sequence from [Thermosynechococcus elongatus] with CL, PG4 and PGE as [ligands]. Full crystallographic information is available from [OCA].
Reference
Antioxidant Dps protein from the thermophilic cyanobacterium Thermosynechococcus elongatus., Franceschini S, Ceci P, Alaleona F, Chiancone E, Ilari A, FEBS J. 2006 Nov;273(21):4913-28. Epub 2006 Oct 3. PMID:17018059
Page seeded by OCA on Mon Oct 29 18:59:41 2007
Categories: Single protein | Thermosynechococcus elongatus | Ceci, P. | Chiancone, E. | Franceschini, S. | Ilari, A. | CL | PG4 | PGE | Dna-binding protein | Dps (dna-binding proteins from starved cells) | Iron binding | Iron-binding/oxidation protein | Stress protein | Thermophilic cyanobacterium | Thermostable protein
