1pek
From Proteopedia
(New page: 200px<br /><applet load="1pek" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pek, resolution 2.2Å" /> '''STRUCTURE OF THE COMP...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1pek.jpg|left|200px]]<br /><applet load="1pek" size=" | + | [[Image:1pek.jpg|left|200px]]<br /><applet load="1pek" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1pek, resolution 2.2Å" /> | caption="1pek, resolution 2.2Å" /> | ||
'''STRUCTURE OF THE COMPLEX OF PROTEINASE K WITH A SUBSTRATE-ANALOGUE HEXA-PEPTIDE INHIBITOR AT 2.2 ANGSTROMS RESOLUTION'''<br /> | '''STRUCTURE OF THE COMPLEX OF PROTEINASE K WITH A SUBSTRATE-ANALOGUE HEXA-PEPTIDE INHIBITOR AT 2.2 ANGSTROMS RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of a transition state/product complex formed by the | + | The crystal structure of a transition state/product complex formed by the interaction between proteinase K and the substrate analogue N-Ac-L-Pro-L-Ala-L-Pro-L-Phe-D-Ala-L-Ala-NH2 has been determined at a resolution of 2.2 A and refined to an R-factor of 0.165 for 12,725 reflections. The inhibitor forms a stable complex through a series of hydrogen bonds with protein atoms and water molecules. The inhibitor is hydrolyzed between Phe 4I and D-Ala5I (I indicates inhibitor). The two fragments are separated by a distance of 3.07 A between the carbonyl carbon and the main chain nitrogen. Both fragments remain bound to the protein. The N-terminal fragment occupies subsites S5 to S1, whereas the C-terminal part is bound in S1' and S2', the first time that electron density for a substrate analogue has been observed in the P1' and P2' sites of a subtilisin-like enzyme. The flexible segments of the substrate recognition sites Gly100-Tyr104 and Ser132-Gly136 move appreciably to accommodate the inhibitor. Biochemical results indicate an inhibition by this specifically designed peptide of 95%. |
==About this Structure== | ==About this Structure== | ||
| - | 1PEK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Active as [http://en.wikipedia.org/wiki/Peptidase_K Peptidase K], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.64 3.4.21.64] Full crystallographic information is available from [http:// | + | 1PEK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Active as [http://en.wikipedia.org/wiki/Peptidase_K Peptidase K], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.64 3.4.21.64] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PEK OCA]. |
==Reference== | ==Reference== | ||
| Line 17: | Line 17: | ||
[[Category: Peters, K.]] | [[Category: Peters, K.]] | ||
[[Category: Saenger, W.]] | [[Category: Saenger, W.]] | ||
| - | [[Category: Singh, T | + | [[Category: Singh, T P.]] |
[[Category: Visanji, M.]] | [[Category: Visanji, M.]] | ||
| - | [[Category: Wilson, K | + | [[Category: Wilson, K S.]] |
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:28:02 2008'' |
Revision as of 12:28, 21 February 2008
|
STRUCTURE OF THE COMPLEX OF PROTEINASE K WITH A SUBSTRATE-ANALOGUE HEXA-PEPTIDE INHIBITOR AT 2.2 ANGSTROMS RESOLUTION
Overview
The crystal structure of a transition state/product complex formed by the interaction between proteinase K and the substrate analogue N-Ac-L-Pro-L-Ala-L-Pro-L-Phe-D-Ala-L-Ala-NH2 has been determined at a resolution of 2.2 A and refined to an R-factor of 0.165 for 12,725 reflections. The inhibitor forms a stable complex through a series of hydrogen bonds with protein atoms and water molecules. The inhibitor is hydrolyzed between Phe 4I and D-Ala5I (I indicates inhibitor). The two fragments are separated by a distance of 3.07 A between the carbonyl carbon and the main chain nitrogen. Both fragments remain bound to the protein. The N-terminal fragment occupies subsites S5 to S1, whereas the C-terminal part is bound in S1' and S2', the first time that electron density for a substrate analogue has been observed in the P1' and P2' sites of a subtilisin-like enzyme. The flexible segments of the substrate recognition sites Gly100-Tyr104 and Ser132-Gly136 move appreciably to accommodate the inhibitor. Biochemical results indicate an inhibition by this specifically designed peptide of 95%.
About this Structure
1PEK is a Single protein structure of sequence from [1]. Active as Peptidase K, with EC number 3.4.21.64 Full crystallographic information is available from OCA.
Reference
Structure of the complex of proteinase K with a substrate analogue hexapeptide inhibitor at 2.2-A resolution., Betzel C, Singh TP, Visanji M, Peters K, Fittkau S, Saenger W, Wilson KS, J Biol Chem. 1993 Jul 25;268(21):15854-8. PMID:8340410
Page seeded by OCA on Thu Feb 21 14:28:02 2008
