2dpe

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|PDB= 2dpe |SIZE=350|CAPTION= <scene name='initialview01'>2dpe</scene>, resolution 2.07&Aring;
|PDB= 2dpe |SIZE=350|CAPTION= <scene name='initialview01'>2dpe</scene>, resolution 2.07&Aring;
|SITE=
|SITE=
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|LIGAND=
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|LIGAND= <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=[[1ljy|1LJY]], [[2esc|2ESC]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2dpe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dpe OCA], [http://www.ebi.ac.uk/pdbsum/2dpe PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2dpe RCSB]</span>
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[[Category: signaling protein]]
[[Category: signaling protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:29:49 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:37:38 2008''

Revision as of 23:37, 30 March 2008


PDB ID 2dpe

Drag the structure with the mouse to rotate
, resolution 2.07Å
Ligands: , ,
Related: 1LJY, 2ESC


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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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