Summary for 2DPE
| Entry DOI | 10.2210/pdb2dpe/pdb |
| Related | 1LJY 2ESC |
| Descriptor | Chitinase-3-like protein 1, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-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 | mammary gland secretion, involution, signaling protein |
| Biological source | Ovis aries (sheep) |
| Total number of polymer chains | 1 |
| Total formula weight | 41523.63 |
| Authors | Srivastava, D.B.,Ethayathulla, A.S.,Kumar, J.,Singh, N.,Sharma, S.,Das, U.,Srinivasan, A.,Singh, T.P. (deposition date: 2006-05-11, release date: 2006-05-30, Last modification date: 2024-10-30) |
| Primary citation | Srivastava, D.B.,Ethayathulla, A.S.,Kumar, J.,Singh, N.,Sharma, S.,Das, U.,Srinivasan, A.,Singh, T.P. Crystal structure of a secretory signalling glycoprotein from sheep at 2.0A resolution J.Struct.Biol., 156:505-516, 2006 Cited by PubMed Abstract: A 40kDa glycoprotein from dry secretion of sheep is implicated as a signaling factor and is named as SPS-40. This protein is secreted only during the early phase of involution when the drastic tissue remodeling occurs in the mammary gland. SPS-40 was purified from sheep dry secretions and crystallized using hanging drop vapour diffusion method. The crystals belong to orthorhombic space group P2(1)2(1)2(1) with cell dimensions, a=62.7A, b=66.4A, c=107.5A. The protein was also cloned for the determination of its complete amino acid sequence. The three-dimensional structure of SPS-40 was determined by X-ray crystallographic method at 2.0A resolution. The structure revealed the presence of an N-linked glycan chain at Asn39. The protein adopts a conformation with a classical (beta/alpha)(8)-barrel fold of triosephosphate isomerase (TIM) (residues 1-237 and 310-360) with an insertion of a small (alpha+beta) domain (residues 240-307) similar to that observed in chitinases. However, the Leu substitution for Glu in the consensus catalytic sequence in SPS-40 causes a loss of chitinase activity. Furthermore, the sugar-binding groove in SPS-40 is distorted considerably from the standard chitin-binding site in chitinase enzymes and hence the binding of chitin-like oligosaccharides is considerably hampered. Three surface loops, His188-His197, Phe202-Arg212 and Phe244-Pro260 have exceptionally high values of B-factors (average=70.5A(2)), indicating the presence of a less defined region. PubMed: 16859926DOI: 10.1016/j.jsb.2006.05.008 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.07 Å) |
Structure validation
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