2bu9: Difference between revisions

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[[Image:2bu9.gif|left|200px]]
{{Seed}}
[[Image:2bu9.png|left|200px]]


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{{STRUCTURE_2bu9|  PDB=2bu9  |  SCENE=  }}  
{{STRUCTURE_2bu9|  PDB=2bu9  |  SCENE=  }}  


'''ISOPENICILLIN N SYNTHASE COMPLEXED WITH L-AMINOADIPOYL-L-CYSTEINYL-L-HEXAFLUOROVALINE'''
===ISOPENICILLIN N SYNTHASE COMPLEXED WITH L-AMINOADIPOYL-L-CYSTEINYL-L-HEXAFLUOROVALINE===




==Overview==
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Isopenicillin N synthase (IPNS) is a non-haem iron oxidase that catalyses the formation of isopenicillin N from the tripeptide delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-valine. In this report, we describe the crystal structure of the enzyme with a non-natural L,L,L-tripeptide substrate, delta-(L-alpha-aminoadipoyl)-L-cysteinyl-L-3,3,3,3',3',3'-hexafluorovaline . This structure reveals a strong binding interaction of the tripeptide within the active site and a unique conformation for the non-natural L,L,L-diastereomer. Taken together, these findings provide a possible rationale for the previously observed inhibitory effects of L,L,L-tripeptide substrates on IPNS activity.
The line below this paragraph, {{ABSTRACT_PUBMED_16143309}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_16143309}}


==About this Structure==
==About this Structure==
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[[Category: Oxygenase]]
[[Category: Oxygenase]]
[[Category: Penicillin biosynthesis]]
[[Category: Penicillin biosynthesis]]
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