1wl7
From Proteopedia
(New page: 200px<br /><applet load="1wl7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wl7, resolution 1.90Å" /> '''Structure of the the...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1wl7.gif|left|200px]]<br /><applet load="1wl7" size=" | + | [[Image:1wl7.gif|left|200px]]<br /><applet load="1wl7" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1wl7, resolution 1.90Å" /> | caption="1wl7, resolution 1.90Å" /> | ||
'''Structure of the thermostable arabinanase'''<br /> | '''Structure of the thermostable arabinanase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of a thermostable endo-1,5-alpha-L-arabinanase, ABN-TS, from Bacillus thermodenitrificans TS-3 was determined at 1.9 A to | + | The crystal structure of a thermostable endo-1,5-alpha-L-arabinanase, ABN-TS, from Bacillus thermodenitrificans TS-3 was determined at 1.9 A to an R-factor of 18.3% and an R-free-factor of 22.5%. The enzyme molecule has a five-bladed beta-propeller fold. The substrate-binding cleft formed across one face of the propeller is open on both sides to allow random binding of several sugar units in the polymeric substrate arabinan. The beta-propeller fold is stabilized through a ring closure. ABN-TS exhibits a new closure-mode involving residues in the N-terminal region: Phe7 to Gly21 exhibit hydrogen bonds and hydrophobic interactions with the first and last blades, and Phe4 links the second and third blades through a hydrogen bond and an aromatic stacking interaction, respectively. The role of the N-terminal region in the thermostability was confirmed with a mutant lacking 16 amino acid residues from the N-terminus of ABN-TS. |
==About this Structure== | ==About this Structure== | ||
| - | 1WL7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_thermodenitrificans Geobacillus thermodenitrificans] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Arabinan_endo-1,5-alpha-L-arabinosidase Arabinan endo-1,5-alpha-L-arabinosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.99 3.2.1.99] Full crystallographic information is available from [http:// | + | 1WL7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_thermodenitrificans Geobacillus thermodenitrificans] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Arabinan_endo-1,5-alpha-L-arabinosidase Arabinan endo-1,5-alpha-L-arabinosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.99 3.2.1.99] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WL7 OCA]. |
==Reference== | ==Reference== | ||
| - | Structural basis for thermostability of endo-1,5-alpha-L-arabinanase from Bacillus thermodenitrificans TS-3., Yamaguchi A, Tada T, Wada K, Nakaniwa T, Kitatani T, Sogabe Y, Takao M, Sakai T, Nishimura K, J Biochem | + | Structural basis for thermostability of endo-1,5-alpha-L-arabinanase from Bacillus thermodenitrificans TS-3., Yamaguchi A, Tada T, Wada K, Nakaniwa T, Kitatani T, Sogabe Y, Takao M, Sakai T, Nishimura K, J Biochem. 2005 May;137(5):587-92. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15944411 15944411] |
[[Category: Arabinan endo-1,5-alpha-L-arabinosidase]] | [[Category: Arabinan endo-1,5-alpha-L-arabinosidase]] | ||
[[Category: Geobacillus thermodenitrificans]] | [[Category: Geobacillus thermodenitrificans]] | ||
| Line 25: | Line 25: | ||
[[Category: thermostable enzyme]] | [[Category: thermostable enzyme]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:45:38 2008'' |
Revision as of 13:45, 21 February 2008
|
Structure of the thermostable arabinanase
Overview
The crystal structure of a thermostable endo-1,5-alpha-L-arabinanase, ABN-TS, from Bacillus thermodenitrificans TS-3 was determined at 1.9 A to an R-factor of 18.3% and an R-free-factor of 22.5%. The enzyme molecule has a five-bladed beta-propeller fold. The substrate-binding cleft formed across one face of the propeller is open on both sides to allow random binding of several sugar units in the polymeric substrate arabinan. The beta-propeller fold is stabilized through a ring closure. ABN-TS exhibits a new closure-mode involving residues in the N-terminal region: Phe7 to Gly21 exhibit hydrogen bonds and hydrophobic interactions with the first and last blades, and Phe4 links the second and third blades through a hydrogen bond and an aromatic stacking interaction, respectively. The role of the N-terminal region in the thermostability was confirmed with a mutant lacking 16 amino acid residues from the N-terminus of ABN-TS.
About this Structure
1WL7 is a Single protein structure of sequence from Geobacillus thermodenitrificans with as ligand. Active as Arabinan endo-1,5-alpha-L-arabinosidase, with EC number 3.2.1.99 Full crystallographic information is available from OCA.
Reference
Structural basis for thermostability of endo-1,5-alpha-L-arabinanase from Bacillus thermodenitrificans TS-3., Yamaguchi A, Tada T, Wada K, Nakaniwa T, Kitatani T, Sogabe Y, Takao M, Sakai T, Nishimura K, J Biochem. 2005 May;137(5):587-92. PMID:15944411
Page seeded by OCA on Thu Feb 21 15:45:38 2008
