2bjf: Difference between revisions

Line 1:

[[Image:2bjf.~~gif~~|left|200px]]

[[Image:2bjf.png|left|200px]]

<!--

Line 9:

Line 10:

~~'''~~CRYSTAL STRUCTURE OF CONJUGATED BILE ACID HYDROLASE FROM CLOSTRIDIUM PERFRINGENS IN COMPLEX WITH REACTION PRODUCTS TAURINE AND DEOXYCHOLATE~~'''~~

===CRYSTAL STRUCTURE OF CONJUGATED BILE ACID HYDROLASE FROM CLOSTRIDIUM PERFRINGENS IN COMPLEX WITH REACTION PRODUCTS TAURINE AND DEOXYCHOLATE===

~~==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.

The line below this paragraph, {{ABSTRACT_PUBMED_15823032}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 15823032 is the PubMed ID number.

-->

==About this Structure==

Line 33:

Line 37:

[[Category: Hydrolase]]

[[Category: Ntn-hydrolase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 20~~:22:22 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:30:58 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:2bjf.gif|left|200px]]
+{{Seed}}
+[[Image:2bjf.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2bjf|  PDB=2bjf  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF CONJUGATED BILE ACID HYDROLASE FROM CLOSTRIDIUM PERFRINGENS IN COMPLEX WITH REACTION PRODUCTS TAURINE AND DEOXYCHOLATE'''
+===CRYSTAL STRUCTURE OF CONJUGATED BILE ACID HYDROLASE FROM CLOSTRIDIUM PERFRINGENS IN COMPLEX WITH REACTION PRODUCTS TAURINE AND DEOXYCHOLATE===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15823032}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15823032 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15823032}}
 ==About this Structure==
@@ Line 33: / Line 37: @@
 [[Category: Hydrolase]]
 [[Category: Ntn-hydrolase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 20:22:22 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:30:58 2008''