Gaur, Vineet ; Chanana, Veenu ; Jain, Abha ; Salunke, Dinakar M. (2011) The structure of a haemopexin-fold protein from cow pea (Vigna unguiculata) suggests functional diversity of haemopexins in plants Acta Crystallographica Section F, 67 (2). pp. 193-200. ISSN 1744-3091
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Official URL: http://onlinelibrary.wiley.com/doi/10.1107/S174430...
Related URL: http://dx.doi.org/10.1107/S1744309110051250
Abstract
The haemopexin fold is present in almost all life forms and is utilized for carrying out diverse physiological functions. The structure of CP4, a haemopexin-fold protein from cow pea (Vigna unguiculata), was determined at 2.1 Å resolution. The protein exists as a monomer both in solution and in the crystal. The structure revealed a typical four-bladed β -propeller topology. The protein exhibits 42% sequence similarity to LS-24 from Lathyrus sativus, with substantial differences in the surface-charge distribution and in the oligomeric state. A structure-based sequence analysis of haemopexin-fold proteins of plant and mammalian origin established a sequence signature associated with the haemopexin motif. This signature sequence enabled the identification of other proteins with possible haemopexin-like topology of both plant and animal origin. Although CP4 shares a structural fold with LS-24 and other haemopexins, biochemical studies indicated possible functional differences between CP4 and LS-24. While both of these proteins exhibit spermine-binding potential, CP4 does not bind to haem, unlike LS-24.
Item Type: | Article |
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Source: | Copyright of this article belongs to John Wiley and Sons. |
Keywords: | CP4; Haemopexin Fold; Vigna Unguiculata |
ID Code: | 52616 |
Deposited On: | 04 Aug 2011 08:06 |
Last Modified: | 04 Aug 2011 08:08 |
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