1skf
From Proteopedia
(New page: 200px<br /> <applet load="1skf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1skf, resolution 2.00Å" /> '''CRYSTAL STRUCTURE O...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1SKF is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Streptomyces_sp. Streptomyces sp.]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.16.4 3.4.16.4]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SKF OCA]]. | + | 1SKF is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Streptomyces_sp. Streptomyces sp.]]. Active as [[http://en.wikipedia.org/wiki/Serine-type_D-Ala-D-Ala_carboxypeptidase Serine-type D-Ala-D-Ala carboxypeptidase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.16.4 3.4.16.4]]. Structure known Active Site: ACT. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SKF OCA]]. |
==Reference== | ==Reference== | ||
The crystal structure of a penicilloyl-serine transferase of intermediate penicillin sensitivity. The DD-transpeptidase of streptomyces K15., Fonze E, Vermeire M, Nguyen-Disteche M, Brasseur R, Charlier P, J Biol Chem. 1999 Jul 30;274(31):21853-60. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10419503 10419503] | The crystal structure of a penicilloyl-serine transferase of intermediate penicillin sensitivity. The DD-transpeptidase of streptomyces K15., Fonze E, Vermeire M, Nguyen-Disteche M, Brasseur R, Charlier P, J Biol Chem. 1999 Jul 30;274(31):21853-60. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10419503 10419503] | ||
| + | [[Category: Serine-type D-Ala-D-Ala carboxypeptidase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptomyces sp.]] | [[Category: Streptomyces sp.]] | ||
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[[Category: serine peptidase]] | [[Category: serine peptidase]] | ||
| - | ''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 10:53:37 2007'' |
Revision as of 08:48, 30 October 2007
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CRYSTAL STRUCTURE OF THE STREPTOMYCES K15 DD-TRANSPEPTIDASE
Overview
The serine DD-transpeptidase/penicillin-binding protein of Streptomyces, K15 catalyzes peptide bond formation in a way that mimics the, penicillin-sensitive peptide cross-linking reaction involved in bacterial, cell wall peptidoglycan assembly. The Streptomyces K15 enzyme is peculiar, in that it can be considered as an intermediate between classical, penicillin-binding proteins, for which benzylpenicillin is a very, efficient inactivator, and the resistant penicillin-binding proteins that, have a low penicillin affinity. With its moderate penicillin sensitivity, the Streptomyces K15 DD-transpeptidase would be helpful in the, understanding of the structure-activity relationship of this, penicillin-recognizing protein superfamily. The structure of the, Streptomyces K15 enzyme has been ... [(full description)]
About this Structure
1SKF is a [Single protein] structure of sequence from [Streptomyces sp.]. Active as [Serine-type D-Ala-D-Ala carboxypeptidase], with EC number [3.4.16.4]. Structure known Active Site: ACT. Full crystallographic information is available from [OCA].
Reference
The crystal structure of a penicilloyl-serine transferase of intermediate penicillin sensitivity. The DD-transpeptidase of streptomyces K15., Fonze E, Vermeire M, Nguyen-Disteche M, Brasseur R, Charlier P, J Biol Chem. 1999 Jul 30;274(31):21853-60. PMID:10419503
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