2hez

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[[Image:2hez.gif|left|200px]]
[[Image:2hez.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2hez |SIZE=350|CAPTION= <scene name='initialview01'>2hez</scene>, resolution 2.50&Aring;
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The line below this paragraph, containing "STRUCTURE_2hez", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= bsh ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=216816 Bifidobacterium longum])
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-->
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|DOMAIN=
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{{STRUCTURE_2hez| PDB=2hez | SCENE= }}
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|RELATEDENTRY=[[2hf0|2HF0]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hez FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hez OCA], [http://www.ebi.ac.uk/pdbsum/2hez PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2hez RCSB]</span>
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}}
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'''Bifidobacterium longum bile salt hydrolase'''
'''Bifidobacterium longum bile salt hydrolase'''
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[[Category: Kumar, R S.]]
[[Category: Kumar, R S.]]
[[Category: Suresh, C G.]]
[[Category: Suresh, C G.]]
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[[Category: alpha]]
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[[Category: Alpha]]
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[[Category: beta]]
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[[Category: Beta]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:12:46 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:29:27 2008''
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Revision as of 03:12, 4 May 2008

Image:2hez.gif

Template:STRUCTURE 2hez

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 Page seeded by OCA on Sun May 4 06:12:46 2008

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