2hez
From Proteopedia
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| - | [[Image:2hez.gif|left|200px]] | + | [[Image:2hez.gif|left|200px]] |
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| - | '''Bifidobacterium longum bile salt hydrolase''' | + | {{Structure |
| + | |PDB= 2hez |SIZE=350|CAPTION= <scene name='initialview01'>2hez</scene>, resolution 2.50Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Choloylglycine_hydrolase Choloylglycine hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.24 3.5.1.24] | ||
| + | |GENE= bsh ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=216816 Bifidobacterium longum]) | ||
| + | }} | ||
| + | |||
| + | '''Bifidobacterium longum bile salt hydrolase''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2HEZ is a [ | + | 2HEZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bifidobacterium_longum Bifidobacterium longum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HEZ OCA]. |
==Reference== | ==Reference== | ||
| - | Structural and functional analysis of a conjugated bile salt hydrolase from Bifidobacterium longum reveals an evolutionary relationship with penicillin V acylase., Kumar RS, Brannigan JA, Prabhune AA, Pundle AV, Dodson GG, Dodson EJ, Suresh CG, J Biol Chem. 2006 Oct 27;281(43):32516-25. Epub 2006 Aug 11. PMID:[http:// | + | Structural and functional analysis of a conjugated bile salt hydrolase from Bifidobacterium longum reveals an evolutionary relationship with penicillin V acylase., Kumar RS, Brannigan JA, Prabhune AA, Pundle AV, Dodson GG, Dodson EJ, Suresh CG, J Biol Chem. 2006 Oct 27;281(43):32516-25. Epub 2006 Aug 11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16905539 16905539] |
[[Category: Bifidobacterium longum]] | [[Category: Bifidobacterium longum]] | ||
[[Category: Choloylglycine hydrolase]] | [[Category: Choloylglycine hydrolase]] | ||
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[[Category: beta]] | [[Category: beta]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:16:12 2008'' |
Revision as of 15:16, 20 March 2008
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| , resolution 2.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | bsh (Bifidobacterium longum) | ||||||
| Activity: | Choloylglycine hydrolase, with EC number 3.5.1.24 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Bifidobacterium longum bile salt hydrolase
Overview
Bile salt hydrolase (BSH) is an enzyme produced by the intestinal microflora that catalyzes the deconjugation of glycine- or taurine-linked bile salts. The crystal structure of BSH reported here from Bifidobacterium longum reveals that it is a member of N-terminal nucleophil hydrolase structural superfamily possessing the characteristic alphabetabetaalpha tetra-lamellar tertiary structure arrangement. Site-directed mutagenesis of the catalytic nucleophil residue, however, shows that it has no role in zymogen processing into its corresponding active form. Substrate specificity was studied using Michaelis-Menten and inhibition kinetics and fluorescence spectroscopy. These data were compared with the specificity profile of BSH from Clostridium perfrigens and pencillin V acylase from Bacillus sphaericus, for both of which the three-dimensional structures are available. Comparative analysis shows a gradation in activity toward common substrates, throwing light on a possible common route toward the evolution of pencillin V acylase and BSH.
About this Structure
2HEZ is a Single protein structure of sequence from Bifidobacterium longum. Full crystallographic information is available from OCA.
Reference
Structural and functional analysis of a conjugated bile salt hydrolase from Bifidobacterium longum reveals an evolutionary relationship with penicillin V acylase., Kumar RS, Brannigan JA, Prabhune AA, Pundle AV, Dodson GG, Dodson EJ, Suresh CG, J Biol Chem. 2006 Oct 27;281(43):32516-25. Epub 2006 Aug 11. PMID:16905539
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