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2bu9

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|PDB= 2bu9 |SIZE=350|CAPTION= <scene name='initialview01'>2bu9</scene>, resolution 1.30&Aring;
|PDB= 2bu9 |SIZE=350|CAPTION= <scene name='initialview01'>2bu9</scene>, resolution 1.30&Aring;
|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+A'>AC1</scene>
|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=HFV:DELTA-(L-ALPHA-AMINOADIPOYL)-L-CYSTEINYL-L-3,3,3,3',3',3'-HEXAFLUOROVALINE'>HFV</scene>
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|LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=HFV:DELTA-(L-ALPHA-AMINOADIPOYL)-L-CYSTEINYL-L-3,3,3,3&#39;,3&#39;,3&#39;-HEXAFLUOROVALINE'>HFV</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Isopenicillin-N_synthase Isopenicillin-N synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.21.3.1 1.21.3.1]
|ACTIVITY= [http://en.wikipedia.org/wiki/Isopenicillin-N_synthase Isopenicillin-N synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.21.3.1 1.21.3.1]
|GENE=
|GENE=
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[[Category: penicillin biosynthesis]]
[[Category: penicillin biosynthesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:06:47 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 14:47:58 2008''

Revision as of 12:48, 23 March 2008


PDB ID 2bu9

Drag the structure with the mouse to rotate
, resolution 1.30Å
Sites:
Ligands: , and
Activity: Isopenicillin-N synthase, with EC number 1.21.3.1
Coordinates: save as pdb, mmCIF, xml



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


Overview

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.

About this Structure

2BU9 is a Single protein structure of sequence from Emericella nidulans. Full crystallographic information is available from OCA.

Reference

Unique binding of a non-natural L,L,L-substrate by isopenicillin N synthase., Howard-Jones AR, Rutledge PJ, Clifton IJ, Adlington RM, Baldwin JE, Biochem Biophys Res Commun. 2005 Oct 21;336(2):702-8. PMID:16143309

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