1mog
From Proteopedia
(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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| - | [[Image:1mog.gif|left|200px]]<br /><applet load="1mog" size=" | + | [[Image:1mog.gif|left|200px]]<br /><applet load="1mog" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1mog, resolution 1.70Å" /> | caption="1mog, resolution 1.70Å" /> | ||
'''Crystal structure of H. salinarum dodecin'''<br /> | '''Crystal structure of H. salinarum dodecin'''<br /> | ||
==Overview== | ==Overview== | ||
| - | A novel, 68 amino acid long flavoprotein called dodecin has been | + | 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== | ==About this Structure== | ||
| - | 1MOG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Halobacterium_salinarum Halobacterium salinarum] with MG, NA, CL and RBF as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1MOG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Halobacterium_salinarum Halobacterium salinarum] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=RBF:'>RBF</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MOG OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bieger, B.]] | [[Category: Bieger, B.]] | ||
| - | [[Category: Essen, L | + | [[Category: Essen, L O.]] |
[[Category: Oesterhelt, D.]] | [[Category: Oesterhelt, D.]] | ||
[[Category: CL]] | [[Category: CL]] | ||
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[[Category: binding site for dimerized riboflavin]] | [[Category: binding site for dimerized riboflavin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:57:19 2008'' |
Revision as of 11:57, 21 February 2008
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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 , , and 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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