1mog
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(New page: 200px<br /><applet load="1mog" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mog, resolution 1.70Å" /> '''Crystal structure of...)
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Revision as of 19:37, 24 November 2007
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Crystal structure of H. salinarum dodecin
Overview
A novel, 68 amino acid long flavoprotein called dodecin has been, discovered in the proteome of Halobacterium salinarum by inverse, structural genomics. The 1.7 A crystal structure of this protein shows a, dodecameric, hollow sphere-like arrangement of the protein subunits., Unlike other known flavoproteins, which bind only monomeric flavin, cofactors, the structure of the dodecin oligomer comprises six riboflavin, dimers. The dimerization of these riboflavins along the re-faces is, mediated by aromatic, antiparallel pi staggering of their isoalloxazine, moieties. A unique aromatic tetrade is formed by further sandwiching of, the riboflavin dimers between the indole groups of two symmetry-related, Trp36s. So far, the dodecins represent the smallest known flavoproteins., Based on the structure and the wide spread occurrences in pathogenic and, soil eubacteria, a function in flavin storage or protection against, radical or oxygenic stress is suggested for the dodecins.
About this Structure
1MOG is a Single protein structure of sequence from Halobacterium salinarum with MG, NA, CL and RBF as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of halophilic dodecin: a novel, dodecameric flavin binding protein from Halobacterium salinarum., Bieger B, Essen LO, Oesterhelt D, Structure. 2003 Apr;11(4):375-85. PMID:12679016
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