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1zu1
From Proteopedia
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'''Solution Structure of the N-terminal Zinc Fingers of the Xenopus laevis double stranded RNA binding protein ZFa''' | '''Solution Structure of the N-terminal Zinc Fingers of the Xenopus laevis double stranded RNA binding protein ZFa''' | ||
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[[Category: Moller, H M.]] | [[Category: Moller, H M.]] | ||
[[Category: Wright, P E.]] | [[Category: Wright, P E.]] | ||
| - | [[Category: | + | [[Category: Helix-loop-helix]] |
| - | [[Category: | + | [[Category: Helix-turn-helix]] |
| - | [[Category: | + | [[Category: Zinc finger protein]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:04:34 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 15:04, 3 May 2008
Solution Structure of the N-terminal Zinc Fingers of the Xenopus laevis double stranded RNA binding protein ZFa
Overview
Several zinc finger proteins have been discovered recently that bind specifically to double-stranded RNA. These include the mammalian JAZ and wig proteins, and the seven-zinc finger protein ZFa from Xenopus laevis. We have determined the solution structure of a 127 residue fragment of ZFa, which consists of two zinc finger domains connected by a linker that remains unstructured in the free protein in solution. The first zinc finger consists of a three-stranded beta-sheet and three helices, while the second finger contains only a two-stranded sheet and two helices. The common structures of the core regions of the two fingers are superimposable. Each finger has a highly electropositive surface that maps to a helix-kink-helix motif. There is no evidence for interactions between the two fingers, consistent with the length (24 residues) and unstructured nature of the intervening linker. Comparison with a number of other proteins shows similarities in the topology and arrangement of secondary structure elements with canonical DNA-binding zinc fingers, with protein interaction motifs such as FOG zinc fingers, and with other DNA-binding and RNA-binding proteins that do not contain zinc. However, in none of these cases does the alignment of these structures with the ZFa zinc fingers produce a consistent picture of a plausible RNA-binding interface. We conclude that the ZFa zinc fingers represent a new motif for the binding of double-stranded RNA.
About this Structure
1ZU1 is a Single protein structure of sequence from Xenopus laevis. Full crystallographic information is available from OCA.
Reference
Solution structure of the N-terminal zinc fingers of the Xenopus laevis double-stranded RNA-binding protein ZFa., Moller HM, Martinez-Yamout MA, Dyson HJ, Wright PE, J Mol Biol. 2005 Aug 26;351(4):718-30. PMID:16051273 Page seeded by OCA on Sat May 3 18:04:34 2008
