2O9O

Crystal Structure of the buffalo Secretory Signalling Glycoprotein at 2.8 A resolution

Replaces:  1SV8

Summary for 2O9O

• Entry DOI: 10.2210/pdb2o9o/pdb
• Related: 2DPE 2ESC
• Descriptor: Chitinase-3-like protein 1, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: spb-40, tim barrel, signaling protein
• Biological source: Bubalus bubalis (water buffalo)
• Total number of polymer chains: 1
• Total formula weight: 41853.06

Authors

Ethayathulla, A.S.,Srivastava, D.B.,Kumar, J.,Sharma, S.,Kaur, P.,Singh, T.P. (deposition date: 2006-12-14, release date: 2007-01-02, Last modification date: 2024-10-30)

Primary citation

Ethayathulla, A.S.,Srivastava, D.B.,Kumar, J.,Saravanan, K.,Bilgrami, S.,Sharma, S.,Kaur, P.,Srinivasan, A.,Singh, T.P.
Structure of the buffalo secretory signalling glycoprotein at 2.8 A resolution
Acta Crystallogr.,Sect.F, 63:258-265, 2007

PubMed Abstract: The crystal structure of a 40 kDa signalling glycoprotein from buffalo (SPB-40) has been determined at 2.8 A 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.

PubMed: 17401190
DOI: 10.1107/S1744309107010445

Experimental method

X-RAY DIFFRACTION (2.8 Å)