1ayy
From Proteopedia
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| , resolution 2.32Å | |||||||
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| Activity: | N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase, with EC number 3.5.1.26 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
GLYCOSYLASPARAGINASE
Overview
The crystal structure of recombinant glycosylasparaginase from Flavobacterium meningosepticum has been determined at 2.32 angstroms resolution. This enzyme is a glycoamidase that cleaves the link between the asparagine and the N-acetylglucosamine of N-linked oligosaccharides and plays a major role in the degradation of glycoproteins. The three-dimensional structure of the bacterial enzyme is very similar to that of the human enzyme, although it lacks the four disulfide bridges found in the human enzyme. The main difference is the absence of a small random coil domain at the end of the alpha-chain that forms part of the substrate binding cleft and that has a role in the stabilization of the tetramer of the human enzyme. The bacterial glycosylasparaginase is observed as an (alphabeta)2-tetramer in the crystal, despite being a dimer in solution. The study of the structure of the bacterial enzyme allows further evaluation of the effects of disease-causing mutations in the human enzyme and confirms the suitability of the bacterial enzyme as a model for functional analysis.
About this Structure
1AYY is a Protein complex structure of sequences from Elizabethkingia meningoseptica. Full crystallographic information is available from OCA.
Reference
Crystal structure of glycosylasparaginase from Flavobacterium meningosepticum., Xuan J, Tarentino AL, Grimwood BG, Plummer TH Jr, Cui T, Guan C, Van Roey P, Protein Sci. 1998 Mar;7(3):774-81. PMID:9541410
Page seeded by OCA on Sun Mar 30 18:50:14 2008
