1k7c
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(New page: 200px<br /><applet load="1k7c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k7c, resolution 1.12Å" /> '''Rhamnogalacturonan a...)
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Revision as of 16:47, 20 November 2007
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Rhamnogalacturonan acetylesterase with seven N-linked carbohydrate residues distributed at two N-glycosylation sites refined at 1.12 A resolution
Overview
The crystal structure of the glycoprotein rhamnogalacturonan, acetylesterase from Aspergillus aculeatus has been refined to a resolution, of 1.12 A using synchrotron data collected at 263 K. Both of the two, putative N-glycosylation sites at Asn104 and Asn182 are glycosylated and, owing to crystal contacts, the glycan structure at Asn182 is exceptionally, well defined in the electron-density maps, showing the six-carbohydrate, structure, Manalpha1-6(Manalpha1-3)Manalpha1-6Manbeta1-4GlcNAcbeta1-4GlcNAcbeta-Asn18, 2. Equivalent carbohydrate residues were restrained to have similar, geometries, but were refined without target values. The refined bond, lengths and angles were compared with the values obtained from, small-molecule studies that form the basis for the dictionaries used for, glycoprotein refinement.
About this Structure
1K7C is a Single protein structure of sequence from Aspergillus aculeatus with NAG and SO4 as ligands. Full crystallographic information is available from OCA.
Reference
A branched N-linked glycan at atomic resolution in the 1.12 A structure of rhamnogalacturonan acetylesterase., Molgaard A, Larsen S, Acta Crystallogr D Biol Crystallogr. 2002 Jan;58(Pt 1):111-9. Epub 2001, Dec 21. PMID:11752785
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