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==Overview==

The white-rot fungus Phanerochaete chrysosporium has two intracellular, beta-glucosidases (BGL1A and BGL1B) belonging to glycoside hydrolase (GH), family 1. BGL1B effectively hydrolyzes cellobiose and cellobionolactone, but BGL1A does not. We have determined the crystal structure of BGL1A in, substrate-free and gluconolactone complexed forms. The overall structure, and the characteristic of subsite -1 (glycone site) were similar to those, of other known GH1 enzymes. The loop regions covering on the, (beta/alpha)(8) barrel was significantly deviated, and they form a unique, subsite +1 (aglycone site) of BGL1A.

The white-rot fungus Phanerochaete chrysosporium has two intracellular beta-glucosidases (BGL1A and BGL1B) belonging to glycoside hydrolase (GH) family 1. BGL1B effectively hydrolyzes cellobiose and cellobionolactone, but BGL1A does not. We have determined the crystal structure of BGL1A in substrate-free and gluconolactone complexed forms. The overall structure and the characteristic of subsite -1 (glycone site) were similar to those of other known GH1 enzymes. The loop regions covering on the (beta/alpha)(8) barrel was significantly deviated, and they form a unique subsite +1 (aglycone site) of BGL1A.

==About this Structure==

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[[Category: tim barrel]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Tue Jan 29 19~~:16:23 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:05:46 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-The white-rot fungus Phanerochaete chrysosporium has two intracellular, beta-glucosidases (BGL1A and BGL1B) belonging to glycoside hydrolase (GH), family 1. BGL1B effectively hydrolyzes cellobiose and cellobionolactone, but BGL1A does not. We have determined the crystal structure of BGL1A in, substrate-free and gluconolactone complexed forms. The overall structure, and the characteristic of subsite -1 (glycone site) were similar to those, of other known GH1 enzymes. The loop regions covering on the, (beta/alpha)(8) barrel was significantly deviated, and they form a unique, subsite +1 (aglycone site) of BGL1A.
+The white-rot fungus Phanerochaete chrysosporium has two intracellular beta-glucosidases (BGL1A and BGL1B) belonging to glycoside hydrolase (GH) family 1. BGL1B effectively hydrolyzes cellobiose and cellobionolactone, but BGL1A does not. We have determined the crystal structure of BGL1A in substrate-free and gluconolactone complexed forms. The overall structure and the characteristic of subsite -1 (glycone site) were similar to those of other known GH1 enzymes. The loop regions covering on the (beta/alpha)(8) barrel was significantly deviated, and they form a unique subsite +1 (aglycone site) of BGL1A.
 ==About this Structure==
@@ Line 27: / Line 27: @@
 [[Category: tim barrel]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 19:16:23 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:05:46 2008''