User:Jung Won Keum/sandbox1
From Proteopedia
(→(S)-2-Hydroxypropylphosphonic acid epoxidase (HppE)) |
(→Structure of HppE) |
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== Structure of HppE == | == Structure of HppE == | ||
| - | The structure of HppE was first solved by Catherine L. Drennan group in 2005. The three-dimensional structure of HppE confirms its identity as a member of the cupin superfamily, possessing the requisite beta-barrel fold in which antiparallel beta-stands are wrapped around a barrel core in a jelly roll variant. The epoxidase is a physiological homotetramer with one iron per monomer1. Each monomer consists of two domains: the alpha-domain, which is all alpha-helical, and a beta-domain, which consists of anti-parallel beta-strands in a jellyroll beta-barrel motif. The facial triad—His 138, Glu 142 and His 180—is housed within the beta-barrel, defining the HppE active site. [[Image: | + | The structure of HppE was first solved by Catherine L. Drennan group in 2005. The three-dimensional structure of HppE confirms its identity as a member of the cupin superfamily, possessing the requisite beta-barrel fold in which antiparallel beta-stands are wrapped around a barrel core in a jelly roll variant. The epoxidase is a physiological homotetramer with one iron per monomer1. Each monomer consists of two domains: the alpha-domain, which is all alpha-helical, and a beta-domain, which consists of anti-parallel beta-strands in a jellyroll beta-barrel motif. The facial triad—His 138, Glu 142 and His 180—is housed within the beta-barrel, defining the HppE active site. [[Image:monomer.jpg]] |
{{STRUCTURE_1zz8 | PDB=1zz8 | SCENE= }} | {{STRUCTURE_1zz8 | PDB=1zz8 | SCENE= }} | ||
Revision as of 22:26, 10 December 2008
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(S)-2-Hydroxypropylphosphonic acid epoxidase (HppE)
(S)-2-Hydroxypropylphosphonic acid epoxidase (HppE) is an O2-dependent, nonheme Fe(II)-containing oxidase that converts (S)-2-hydroxypropylphosphonic acid ((S)-HPP) to the regio- and enantiomerically specific epoxide, fosfomycin. Fosfomycin ((1R,2S)-epoxypropylphosphonic acid, 1) is an antibiotic used to treat lower urinary tract infections. The biological target of fosfomycin has been identified as UDP-α-d-GlcNAc-O-enolpyruvoyl1 transferase, which catalyzes the attachment of phosphoenolpyruvate to UDP-α-d-GlcNAc, a key step in the assembly of the peptidoglycan layer within the bacterial cell wall. HppE involves in the reaction where(S)-2-hydroxypropylphosphonic acid (S-HPP) is converted into the epoxide fosfomycin via an oxidative cyclization reaction with retention of the substrate hydroxyl oxygen atom.
Structure of HppE
The structure of HppE was first solved by Catherine L. Drennan group in 2005. The three-dimensional structure of HppE confirms its identity as a member of the cupin superfamily, possessing the requisite beta-barrel fold in which antiparallel beta-stands are wrapped around a barrel core in a jelly roll variant. The epoxidase is a physiological homotetramer with one iron per monomer1. Each monomer consists of two domains: the alpha-domain, which is all alpha-helical, and a beta-domain, which consists of anti-parallel beta-strands in a jellyroll beta-barrel motif. The facial triad—His 138, Glu 142 and His 180—is housed within the beta-barrel, defining the HppE active site. 
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| 1zz8, resolution 2.30Å () | |||||||||
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| Ligands: | , | ||||||||
| Gene: | fom4 (Streptomyces wedmorensis) | ||||||||
| Related: | 1zz6, 1zz7, 1zz9, 1zzb, 1zzc | ||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
