2bjf: Difference between revisions

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==Overview==

Bacterial bile salt hydrolases catalyze the degradation of conjugated bile, acids in the mammalian gut. The crystal structures of conjugated bile acid, hydrolase (CBAH) from Clostridium perfringens as apoenzyme and in complex, with taurodeoxycholate that was hydrolyzed to the reaction products, taurine and deoxycholate are described here at 2.1 and 1.7 A resolution, respectively. The crystal structures reveal close relationship between, CBAH and penicillin V acylase from Bacillus sphaericus. This similarity, together with the N-terminal cysteine classifies CBAH as a member of the, N-terminal nucleophile (Ntn) hydrolase superfamily. Both crystal, structures show an identical homotetrameric organization with dihedral, (D(2) or 222) point group symmetry. The structure analysis of C., perfringens CBAH identifies critical residues in catalysis, substrate, recognition, and tetramer formation which may serve in further biochemical, characterization of bile acid hydrolases.

Bacterial bile salt hydrolases catalyze the degradation of conjugated bile acids in the mammalian gut. The crystal structures of conjugated bile acid hydrolase (CBAH) from Clostridium perfringens as apoenzyme and in complex with taurodeoxycholate that was hydrolyzed to the reaction products taurine and deoxycholate are described here at 2.1 and 1.7 A resolution, respectively. The crystal structures reveal close relationship between CBAH and penicillin V acylase from Bacillus sphaericus. This similarity together with the N-terminal cysteine classifies CBAH as a member of the N-terminal nucleophile (Ntn) hydrolase superfamily. Both crystal structures show an identical homotetrameric organization with dihedral (D(2) or 222) point group symmetry. The structure analysis of C. perfringens CBAH identifies critical residues in catalysis, substrate recognition, and tetramer formation which may serve in further biochemical characterization of bile acid hydrolases.

==About this Structure==

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[[Category: Clostridium perfringens]]

[[Category: Single protein]]

[[Category: Coleman, J.P.]]

[[Category: Coleman, J P.]]

[[Category: Moeller, H.Von.]]

[[Category: Moeller, H Von.]]

[[Category: Rossocha, M.]]

[[Category: Saenger, W.]]

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[[Category: ntn-hydrolase]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-Bacterial bile salt hydrolases catalyze the degradation of conjugated bile, acids in the mammalian gut. The crystal structures of conjugated bile acid, hydrolase (CBAH) from Clostridium perfringens as apoenzyme and in complex, with taurodeoxycholate that was hydrolyzed to the reaction products, taurine and deoxycholate are described here at 2.1 and 1.7 A resolution, respectively. The crystal structures reveal close relationship between, CBAH and penicillin V acylase from Bacillus sphaericus. This similarity, together with the N-terminal cysteine classifies CBAH as a member of the, N-terminal nucleophile (Ntn) hydrolase superfamily. Both crystal, structures show an identical homotetrameric organization with dihedral, (D(2) or 222) point group symmetry. The structure analysis of C., perfringens CBAH identifies critical residues in catalysis, substrate, recognition, and tetramer formation which may serve in further biochemical, characterization of bile acid hydrolases.
+Bacterial bile salt hydrolases catalyze the degradation of conjugated bile acids in the mammalian gut. The crystal structures of conjugated bile acid hydrolase (CBAH) from Clostridium perfringens as apoenzyme and in complex with taurodeoxycholate that was hydrolyzed to the reaction products taurine and deoxycholate are described here at 2.1 and 1.7 A resolution, respectively. The crystal structures reveal close relationship between CBAH and penicillin V acylase from Bacillus sphaericus. This similarity together with the N-terminal cysteine classifies CBAH as a member of the N-terminal nucleophile (Ntn) hydrolase superfamily. Both crystal structures show an identical homotetrameric organization with dihedral (D(2) or 222) point group symmetry. The structure analysis of C. perfringens CBAH identifies critical residues in catalysis, substrate recognition, and tetramer formation which may serve in further biochemical characterization of bile acid hydrolases.
 ==About this Structure==
@@ Line 14: / Line 14: @@
 [[Category: Clostridium perfringens]]
 [[Category: Single protein]]
-[[Category: Coleman, J.P.]]
+[[Category: Coleman, J P.]]
-[[Category: Moeller, H.Von.]]
+[[Category: Moeller, H Von.]]
 [[Category: Rossocha, M.]]
 [[Category: Saenger, W.]]
@@ Line 28: / Line 28: @@
 [[Category: ntn-hydrolase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:24:52 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:38:29 2008''