1wzz
From Proteopedia
(New page: 200px<br /><applet load="1wzz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wzz, resolution 1.65Å" /> '''Structure of endo-be...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1wzz.gif|left|200px]]<br /><applet load="1wzz" size=" | + | [[Image:1wzz.gif|left|200px]]<br /><applet load="1wzz" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1wzz, resolution 1.65Å" /> | caption="1wzz, resolution 1.65Å" /> | ||
'''Structure of endo-beta-1,4-glucanase CMCax from Acetobacter xylinum'''<br /> | '''Structure of endo-beta-1,4-glucanase CMCax from Acetobacter xylinum'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Previous studies have demonstrated that endoglucanase is required for | + | Previous studies have demonstrated that endoglucanase is required for cellulose biosynthesis both in bacteria and plants. However, it has yet to be elucidated how the endoglucanases function in the mechanism of cellulose biosynthesis. Here we describe the crystal structure of the cellulose biosynthesis-related endo-beta-1,47-glucanase (CMCax; EC 3.2.1.4) from the cellulose-producing Gramnegative bacterium, Acetobacter xylinum (= Gluconacetobacter xylinus), determined at 1.65-A resolution. CMCax falls into the glycoside hydrolase family 8 (GH-8), and the structure showed that the overall fold of the CMCax is similar to those of other glycoside hydrolases belonging to GH-8. Structure comparison with Clostridium thermocellum CelA, the best characterized GH-8 endoglucanase, revealed that sugar recognition subsite +3 is completely missing in CMCax. The absence of the subsite +3 leads to significant broadness of the cleft at the cellooligosaccharide reducing-end side. CMCax is known to be a secreted enzyme and is present in the culture medium. However, electron microscopic analysis using immunostaining clearly demonstrated that a portion of CMCax is localized to the cell surface, suggesting a link with other known membrane-anchored endoglucanases that are required for cellulose biosynthesis. |
==About this Structure== | ==About this Structure== | ||
| - | 1WZZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gluconacetobacter_xylinus Gluconacetobacter xylinus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] Full crystallographic information is available from [http:// | + | 1WZZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gluconacetobacter_xylinus Gluconacetobacter xylinus] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZZ OCA]. |
==Reference== | ==Reference== | ||
| Line 16: | Line 16: | ||
[[Category: Kawano, S.]] | [[Category: Kawano, S.]] | ||
[[Category: Munekata, M.]] | [[Category: Munekata, M.]] | ||
| - | [[Category: SGC, Structural | + | [[Category: SGC, Structural Genomics Consortium.]] |
[[Category: Satoh, Y.]] | [[Category: Satoh, Y.]] | ||
[[Category: Tajima, K.]] | [[Category: Tajima, K.]] | ||
| Line 29: | Line 29: | ||
[[Category: structural genomics consortium for research on gene expression system]] | [[Category: structural genomics consortium for research on gene expression system]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:49:44 2008'' |
Revision as of 13:49, 21 February 2008
|
Structure of endo-beta-1,4-glucanase CMCax from Acetobacter xylinum
Overview
Previous studies have demonstrated that endoglucanase is required for cellulose biosynthesis both in bacteria and plants. However, it has yet to be elucidated how the endoglucanases function in the mechanism of cellulose biosynthesis. Here we describe the crystal structure of the cellulose biosynthesis-related endo-beta-1,47-glucanase (CMCax; EC 3.2.1.4) from the cellulose-producing Gramnegative bacterium, Acetobacter xylinum (= Gluconacetobacter xylinus), determined at 1.65-A resolution. CMCax falls into the glycoside hydrolase family 8 (GH-8), and the structure showed that the overall fold of the CMCax is similar to those of other glycoside hydrolases belonging to GH-8. Structure comparison with Clostridium thermocellum CelA, the best characterized GH-8 endoglucanase, revealed that sugar recognition subsite +3 is completely missing in CMCax. The absence of the subsite +3 leads to significant broadness of the cleft at the cellooligosaccharide reducing-end side. CMCax is known to be a secreted enzyme and is present in the culture medium. However, electron microscopic analysis using immunostaining clearly demonstrated that a portion of CMCax is localized to the cell surface, suggesting a link with other known membrane-anchored endoglucanases that are required for cellulose biosynthesis.
About this Structure
1WZZ is a Single protein structure of sequence from Gluconacetobacter xylinus with as ligand. Active as Cellulase, with EC number 3.2.1.4 Full crystallographic information is available from OCA.
Reference
Structural characterization of the Acetobacter xylinum endo-beta-1,4-glucanase CMCax required for cellulose biosynthesis., Yasutake Y, Kawano S, Tajima K, Yao M, Satoh Y, Munekata M, Tanaka I, Proteins. 2006 Sep 1;64(4):1069-77. PMID:16804941
Page seeded by OCA on Thu Feb 21 15:49:44 2008
Categories: Cellulase | Gluconacetobacter xylinus | Single protein | Kawano, S. | Munekata, M. | SGC, Structural Genomics Consortium. | Satoh, Y. | Tajima, K. | Tanaka, I. | Yao, M. | Yasutake, Y. | SO4 | (alpha/alpha)6 barrel | Glycoside hydrolase family 8 (gh-8) | Sgcges | Structural genomics | Structural genomics consortium for research on gene expression system
