1uvh
From Proteopedia
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[[Category: dna protection from oxidative damage]] | [[Category: dna protection from oxidative damage]] | ||
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Revision as of 14:07, 30 October 2007
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X-RAY STRUCTURE OF DPS FROM MYCOBACTERIUM SMEGMATIS
Overview
The structure and function of Mycobacterium smegmatis Dps (DNA-binding, proteins from starved cells) and of the protein studied by Gupta and, Chatterji, in which the C terminus that is used for binding DNA contains a, histidine tag, have been characterized in parallel. The native dodecamer, dissociated reversibly into dimers above pH 7.5 and below pH 6.0, with, apparent pK(a) values of approximately 7.65 and 4.75; at pH approximately, 4.0, dimers formed monomers. Based on structural analysis, the two, dissociation steps have been attributed to breakage of the salt bridges, between Glu(157) and Arg(99) located at the 3-fold symmetry axes and to, protonation of Asp(66) hydrogen-bonded to Lys(36) across the dimer, interface, respectively. The C-terminal tag did not affect subunit, ... [(full description)]
About this Structure
1UVH is a [Single protein] structure of sequence from [Mycobacterium smegmatis] with FE as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Reassessment of protein stability, DNA binding, and protection of Mycobacterium smegmatis Dps., Ceci P, Ilari A, Falvo E, Giangiacomo L, Chiancone E, J Biol Chem. 2005 Oct 14;280(41):34776-85. Epub 2005 Jul 19. PMID:16030020
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