2bu9
From Proteopedia
(New page: 200px<br /> <applet load="2bu9" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bu9, resolution 1.30Å" /> '''ISOPENICILLIN N SYN...) |
|||
| Line 8: | Line 8: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2BU9 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Emericella_nidulans Emericella nidulans]] with FE, SO4 and HFV as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.21.3.1 1.21.3.1]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BU9 OCA]]. | + | 2BU9 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Emericella_nidulans Emericella nidulans]] with FE, SO4 and HFV as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[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]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BU9 OCA]]. |
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16143309 16143309] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16143309 16143309] | ||
[[Category: Emericella nidulans]] | [[Category: Emericella nidulans]] | ||
| + | [[Category: Isopenicillin-N synthase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Adlington, R.M.]] | [[Category: Adlington, R.M.]] | ||
| Line 28: | Line 29: | ||
[[Category: penicillin biosynthesis]] | [[Category: penicillin biosynthesis]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:23:16 2007'' |
Revision as of 09:18, 30 October 2007
|
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] with FE, SO4 and HFV as [ligands]. Active as [Isopenicillin-N synthase], with EC number [1.21.3.1]. Structure known Active Site: AC1. 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
Page seeded by OCA on Tue Oct 30 11:23:16 2007
