2gj2

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(New page: 200px<br /><applet load="2gj2" size="350" color="white" frame="true" align="right" spinBox="true" caption="2gj2, resolution 2.35&Aring;" /> '''Crystal Structure of...)
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==Overview==
==Overview==
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White spot syndrome virus (WSSV) is a major pathogen in shrimp, aquaculture. VP9, a full-length protein of WSSV, encoded by open reading, frame wsv230, was identified for the first time in the infected Penaeus, monodon shrimp tissues, gill, and stomach as a novel, nonstructural, protein by Western blotting, mass spectrometry, and immunoelectron, microscopy. Real-time reverse transcription-PCR demonstrated that the, transcription of VP9 started from the early to the late stage of WSSV, infection as a major mRNA species. The structure of full-length VP9 was, determined by both X-ray and nuclear magnetic resonance (NMR) techniques., It is the first structure to be reported for WSSV proteins. The crystal, structure of VP9 revealed a ferredoxin fold with divalent metal ion, binding sites. Cadmium sulfate was found to be essential for, crystallization. The Cd2+ ions were bound between the monomer interfaces, of the homodimer. Various divalent metal ions have been titrated against, VP9, and their interactions were analyzed using NMR spectroscopy. The, titration data indicated that VP9 binds with both Zn2+ and Cd2+. VP9, adopts a similar fold as the DNA binding domain of the papillomavirus E2, protein. Based on our present investigations, we hypothesize that VP9, might be involved in the transcriptional regulation of WSSV, a function, similar to that of the E2 protein during papillomavirus infection of the, host cells.
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White spot syndrome virus (WSSV) is a major pathogen in shrimp aquaculture. VP9, a full-length protein of WSSV, encoded by open reading frame wsv230, was identified for the first time in the infected Penaeus monodon shrimp tissues, gill, and stomach as a novel, nonstructural protein by Western blotting, mass spectrometry, and immunoelectron microscopy. Real-time reverse transcription-PCR demonstrated that the transcription of VP9 started from the early to the late stage of WSSV infection as a major mRNA species. The structure of full-length VP9 was determined by both X-ray and nuclear magnetic resonance (NMR) techniques. It is the first structure to be reported for WSSV proteins. The crystal structure of VP9 revealed a ferredoxin fold with divalent metal ion binding sites. Cadmium sulfate was found to be essential for crystallization. The Cd2+ ions were bound between the monomer interfaces of the homodimer. Various divalent metal ions have been titrated against VP9, and their interactions were analyzed using NMR spectroscopy. The titration data indicated that VP9 binds with both Zn2+ and Cd2+. VP9 adopts a similar fold as the DNA binding domain of the papillomavirus E2 protein. Based on our present investigations, we hypothesize that VP9 might be involved in the transcriptional regulation of WSSV, a function similar to that of the E2 protein during papillomavirus infection of the host cells.
==About this Structure==
==About this Structure==
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[[Category: Shrimp white spot syndrome virus]]
[[Category: Shrimp white spot syndrome virus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Hew, C.L.]]
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[[Category: Hew, C L.]]
[[Category: Liu, Y.]]
[[Category: Liu, Y.]]
[[Category: Sivaraman, J.]]
[[Category: Sivaraman, J.]]
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[[Category: Song, J.X.]]
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[[Category: Song, J X.]]
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[[Category: Wu, J.L.]]
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[[Category: Wu, J L.]]
[[Category: CD]]
[[Category: CD]]
[[Category: ferredoxin fold]]
[[Category: ferredoxin fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 20:00:49 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:32:09 2008''

Revision as of 15:32, 21 February 2008


2gj2, resolution 2.35Å

Drag the structure with the mouse to rotate

Crystal Structure of VP9 from White Spot Syndrome Virus

Overview

White spot syndrome virus (WSSV) is a major pathogen in shrimp aquaculture. VP9, a full-length protein of WSSV, encoded by open reading frame wsv230, was identified for the first time in the infected Penaeus monodon shrimp tissues, gill, and stomach as a novel, nonstructural protein by Western blotting, mass spectrometry, and immunoelectron microscopy. Real-time reverse transcription-PCR demonstrated that the transcription of VP9 started from the early to the late stage of WSSV infection as a major mRNA species. The structure of full-length VP9 was determined by both X-ray and nuclear magnetic resonance (NMR) techniques. It is the first structure to be reported for WSSV proteins. The crystal structure of VP9 revealed a ferredoxin fold with divalent metal ion binding sites. Cadmium sulfate was found to be essential for crystallization. The Cd2+ ions were bound between the monomer interfaces of the homodimer. Various divalent metal ions have been titrated against VP9, and their interactions were analyzed using NMR spectroscopy. The titration data indicated that VP9 binds with both Zn2+ and Cd2+. VP9 adopts a similar fold as the DNA binding domain of the papillomavirus E2 protein. Based on our present investigations, we hypothesize that VP9 might be involved in the transcriptional regulation of WSSV, a function similar to that of the E2 protein during papillomavirus infection of the host cells.

About this Structure

2GJ2 is a Single protein structure of sequence from Shrimp white spot syndrome virus with as ligand. Full crystallographic information is available from OCA.

Reference

Identification of a novel nonstructural protein, VP9, from white spot syndrome virus: its structure reveals a ferredoxin fold with specific metal binding sites., Liu Y, Wu J, Song J, Sivaraman J, Hew CL, J Virol. 2006 Nov;80(21):10419-27. Epub 2006 Sep 6. PMID:16956937

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