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2dpe

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==Overview==
==Overview==
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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.
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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.
==About this Structure==
==About this Structure==
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2DPE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ovis_aries Ovis aries]. This structure superseeds the now removed PDB entry 1R2V. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DPE OCA].
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2DPE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ovis_aries Ovis aries]. This structure supersedes the now removed PDB entry 1R2V. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DPE OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Das, U.]]
[[Category: Das, U.]]
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[[Category: Ethayathulla, A.S.]]
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[[Category: Ethayathulla, A S.]]
[[Category: Kumar, J.]]
[[Category: Kumar, J.]]
[[Category: Sharma, S.]]
[[Category: Sharma, S.]]
[[Category: Singh, N.]]
[[Category: Singh, N.]]
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[[Category: Singh, T.P.]]
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[[Category: Singh, T P.]]
[[Category: Srinivasan, A.]]
[[Category: Srinivasan, A.]]
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[[Category: Srivastava, D.B.]]
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[[Category: Srivastava, D B.]]
[[Category: involution]]
[[Category: involution]]
[[Category: mammary gland secretion]]
[[Category: mammary gland secretion]]
[[Category: signaling protein]]
[[Category: signaling protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:14:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:01:10 2008''

Revision as of 15:01, 21 February 2008


2dpe, resolution 2.07Å

Drag the structure with the mouse to rotate

Crystal structure of a secretory 40KDA glycoprotein from sheep at 2.0A resolution

Overview

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.

About this Structure

2DPE is a Single protein structure of sequence from Ovis aries. This structure supersedes the now removed PDB entry 1R2V. Full crystallographic information is available from OCA.

Reference

Crystal structure of a secretory signalling glycoprotein from sheep at 2.0A resolution., Srivastava DB, Ethayathulla AS, Kumar J, Singh N, Sharma S, Das U, Srinivasan A, Singh TP, J Struct Biol. 2006 Dec;156(3):505-16. Epub 2006 Jun 8. PMID:16859926

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