1nkg
From Proteopedia
(New page: 200px<br /><applet load="1nkg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nkg, resolution 1.50Å" /> '''Rhamnogalacturonan l...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1nkg.gif|left|200px]]<br /><applet load="1nkg" size=" | + | [[Image:1nkg.gif|left|200px]]<br /><applet load="1nkg" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1nkg, resolution 1.50Å" /> | caption="1nkg, resolution 1.50Å" /> | ||
'''Rhamnogalacturonan lyase from Aspergillus aculeatus'''<br /> | '''Rhamnogalacturonan lyase from Aspergillus aculeatus'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Rhamnogalacturonan lyase (RG-lyase) specifically recognizes and cleaves | + | Rhamnogalacturonan lyase (RG-lyase) specifically recognizes and cleaves alpha-1,4 glycosidic bonds between L-rhamnose and D-galacturonic acids in the backbone of rhamnogalacturonan-I, a major component of the plant cell wall polysaccharide, pectin. The three-dimensional structure of RG-lyase from Aspergillus aculeatus has been determined to 1.5 A resolution representing the first known structure from polysaccharide lyase family 4 and of an enzyme with this catalytic specificity. The 508-amino acid polypeptide displays a unique arrangement of three distinct modular domains. Each domain shows structural homology to non-catalytic domains from other carbohydrate active enzymes. |
==About this Structure== | ==About this Structure== | ||
| - | 1NKG 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 CA and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1NKG 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=CA:'>CA</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=1NKG OCA]. |
==Reference== | ==Reference== | ||
| Line 16: | Line 16: | ||
[[Category: Kadirvelraj, R.]] | [[Category: Kadirvelraj, R.]] | ||
[[Category: Larsen, S.]] | [[Category: Larsen, S.]] | ||
| - | [[Category: McDonough, M | + | [[Category: McDonough, M A.]] |
| - | [[Category: Poulsen, J | + | [[Category: Poulsen, J C.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
| Line 24: | Line 24: | ||
[[Category: polysaccharide lyase]] | [[Category: polysaccharide lyase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:07:07 2008'' |
Revision as of 12:07, 21 February 2008
|
Rhamnogalacturonan lyase from Aspergillus aculeatus
Overview
Rhamnogalacturonan lyase (RG-lyase) specifically recognizes and cleaves alpha-1,4 glycosidic bonds between L-rhamnose and D-galacturonic acids in the backbone of rhamnogalacturonan-I, a major component of the plant cell wall polysaccharide, pectin. The three-dimensional structure of RG-lyase from Aspergillus aculeatus has been determined to 1.5 A resolution representing the first known structure from polysaccharide lyase family 4 and of an enzyme with this catalytic specificity. The 508-amino acid polypeptide displays a unique arrangement of three distinct modular domains. Each domain shows structural homology to non-catalytic domains from other carbohydrate active enzymes.
About this Structure
1NKG is a Single protein structure of sequence from Aspergillus aculeatus with and as ligands. Full crystallographic information is available from OCA.
Reference
Rhamnogalacturonan lyase reveals a unique three-domain modular structure for polysaccharide lyase family 4., McDonough MA, Kadirvelraj R, Harris P, Poulsen JC, Larsen S, FEBS Lett. 2004 May 7;565(1-3):188-94. PMID:15135077
Page seeded by OCA on Thu Feb 21 14:07:07 2008
