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Title: Structure of the buffalo secretory signalling glycoprotein at 2.8 Å resolution

Abstract

The crystal structure of a signalling glycoprotein isolated from buffalo dry secretions (SPB-40) has been determined at 2.8 Å resolution. Two unique residues, Tyr120 and Glu269, found in SPB-40 distort the shape of the sugar-binding groove considerably. The water structure in the groove is also different. The conformations of three flexible loops, His188–His197, Phe202–Arg212 and Tyr244–Pro260, also differ from those found in other structurally similar proteins. The crystal structure of a 40 kDa signalling glycoprotein from buffalo (SPB-40) has been determined at 2.8 Å resolution. SPB-40 acts as a protective signalling factor by binding to viable cells during the early phase of involution, during which extensive tissue remodelling occurs. It was isolated from the dry secretions of Murrah buffalo. It was purified and crystallized using the hanging-drop vapour-diffusion method with 19% ethanol as the precipitant. The protein was also cloned and its complete nucleotide and amino-acid sequences were determined. When compared with the sequences of other members of the family, the sequence of SPB-40 revealed two very important mutations in the sugar-binding region, in which Tyr120 changed to Trp120 and Glu269 changed to Trp269. The structure showed a significant distortion in the shape of the sugar-binding groove. The water structuremore » in the groove is also drastically altered. The folding of the protein chain in the flexible region comprising segments His188–His197, Phe202–Arg212 and Tyr244–Pro260 shows large variations when compared with other proteins of the family.« less

Authors:
; ; ; ; ; ; ; ;  [1]
  1. Department of Biophysics, All India Institute of Medical Sciences, New Delhi 110029 (India)
Publication Date:
OSTI Identifier:
22360296
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 63; Journal Issue: Pt 4; Other Information: PMCID: PMC2330205; PMID: 17401190; PUBLISHER-ID: en5226; OAI: oai:pubmedcentral.nih.gov:2330205; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTAL STRUCTURE; DIFFUSION; ETHANOL; RESOLUTION; SACCHAROSE; SHAPE; VARIATIONS; WATER

Citation Formats

Ethayathulla, Abdul S., Srivastava, Devendra B., Kumar, Janesh, Saravanan, Kolandaivelu, Bilgrami, Sameeta, Sharma, Sujata, Kaur, Punit, Srinivasan, Alagiri, and Singh, Tej P., E-mail: tps@aiims.aiims.ac.in. Structure of the buffalo secretory signalling glycoprotein at 2.8 Å resolution. United Kingdom: N. p., 2007. Web. doi:10.1107/S1744309107010445.
Ethayathulla, Abdul S., Srivastava, Devendra B., Kumar, Janesh, Saravanan, Kolandaivelu, Bilgrami, Sameeta, Sharma, Sujata, Kaur, Punit, Srinivasan, Alagiri, & Singh, Tej P., E-mail: tps@aiims.aiims.ac.in. Structure of the buffalo secretory signalling glycoprotein at 2.8 Å resolution. United Kingdom. doi:10.1107/S1744309107010445.
Ethayathulla, Abdul S., Srivastava, Devendra B., Kumar, Janesh, Saravanan, Kolandaivelu, Bilgrami, Sameeta, Sharma, Sujata, Kaur, Punit, Srinivasan, Alagiri, and Singh, Tej P., E-mail: tps@aiims.aiims.ac.in. Sun . "Structure of the buffalo secretory signalling glycoprotein at 2.8 Å resolution". United Kingdom. doi:10.1107/S1744309107010445.
@article{osti_22360296,
title = {Structure of the buffalo secretory signalling glycoprotein at 2.8 Å resolution},
author = {Ethayathulla, Abdul S. and Srivastava, Devendra B. and Kumar, Janesh and Saravanan, Kolandaivelu and Bilgrami, Sameeta and Sharma, Sujata and Kaur, Punit and Srinivasan, Alagiri and Singh, Tej P., E-mail: tps@aiims.aiims.ac.in},
abstractNote = {The crystal structure of a signalling glycoprotein isolated from buffalo dry secretions (SPB-40) has been determined at 2.8 Å resolution. Two unique residues, Tyr120 and Glu269, found in SPB-40 distort the shape of the sugar-binding groove considerably. The water structure in the groove is also different. The conformations of three flexible loops, His188–His197, Phe202–Arg212 and Tyr244–Pro260, also differ from those found in other structurally similar proteins. The crystal structure of a 40 kDa signalling glycoprotein from buffalo (SPB-40) has been determined at 2.8 Å resolution. SPB-40 acts as a protective signalling factor by binding to viable cells during the early phase of involution, during which extensive tissue remodelling occurs. It was isolated from the dry secretions of Murrah buffalo. It was purified and crystallized using the hanging-drop vapour-diffusion method with 19% ethanol as the precipitant. The protein was also cloned and its complete nucleotide and amino-acid sequences were determined. When compared with the sequences of other members of the family, the sequence of SPB-40 revealed two very important mutations in the sugar-binding region, in which Tyr120 changed to Trp120 and Glu269 changed to Trp269. The structure showed a significant distortion in the shape of the sugar-binding groove. The water structure in the groove is also drastically altered. The folding of the protein chain in the flexible region comprising segments His188–His197, Phe202–Arg212 and Tyr244–Pro260 shows large variations when compared with other proteins of the family.},
doi = {10.1107/S1744309107010445},
journal = {Acta Crystallographica. Section F},
number = Pt 4,
volume = 63,
place = {United Kingdom},
year = {Sun Apr 01 00:00:00 EDT 2007},
month = {Sun Apr 01 00:00:00 EDT 2007}
}