2bjf: Difference between revisions

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==About this Structure==
==About this Structure==
2BJF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_perfringens Clostridium perfringens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BJF OCA].  
2BJF is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_perfringens Clostridium perfringens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BJF OCA].  


==Reference==
==Reference==
Conjugated bile acid hydrolase is a tetrameric N-terminal thiol hydrolase with specific recognition of its cholyl but not of its tauryl product., Rossocha M, Schultz-Heienbrok R, von Moeller H, Coleman JP, Saenger W, Biochemistry. 2005 Apr 19;44(15):5739-48. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15823032 15823032]
<ref group="xtra">PMID:15823032</ref><references group="xtra"/>
[[Category: Choloylglycine hydrolase]]
[[Category: Choloylglycine hydrolase]]
[[Category: Clostridium perfringens]]
[[Category: Clostridium perfringens]]
[[Category: Single protein]]
[[Category: Coleman, J P.]]
[[Category: Coleman, J P.]]
[[Category: Moeller, H Von.]]
[[Category: Moeller, H Von.]]
Line 38: Line 37:
[[Category: Ntn-hydrolase]]
[[Category: Ntn-hydrolase]]


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Revision as of 09:28, 16 February 2009

File:2bjf.png

Template:STRUCTURE 2bjf

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

Template:ABSTRACT PUBMED 15823032

About this Structure

2BJF is a 1 chain structure of sequence from Clostridium perfringens. Full crystallographic information is available from OCA.

Reference

  1. Rossocha M, Schultz-Heienbrok R, von Moeller H, Coleman JP, Saenger W. Conjugated bile acid hydrolase is a tetrameric N-terminal thiol hydrolase with specific recognition of its cholyl but not of its tauryl product. Biochemistry. 2005 Apr 19;44(15):5739-48. PMID:15823032 doi:https://dx.doi.org/10.1021/bi0473206

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