1k7c
From Proteopedia
(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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| - | [[Image:1k7c.jpg|left|200px]]<br /><applet load="1k7c" size=" | + | [[Image:1k7c.jpg|left|200px]]<br /><applet load="1k7c" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1k7c, resolution 1.12Å" /> | caption="1k7c, resolution 1.12Å" /> | ||
'''Rhamnogalacturonan acetylesterase with seven N-linked carbohydrate residues distributed at two N-glycosylation sites refined at 1.12 A resolution'''<br /> | '''Rhamnogalacturonan acetylesterase with seven N-linked carbohydrate residues distributed at two N-glycosylation sites refined at 1.12 A resolution'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the glycoprotein rhamnogalacturonan | + | 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== | ==About this Structure== | ||
| - | 1K7C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_aculeatus Aspergillus aculeatus] with NAG and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1K7C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_aculeatus Aspergillus aculeatus] with <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K7C OCA]. |
==Reference== | ==Reference== | ||
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[[Category: sgnh-hydrolase]] | [[Category: sgnh-hydrolase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:30:55 2008'' |
Revision as of 11:30, 21 February 2008
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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 and 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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