1ot5
From Proteopedia
(New page: 200px<br /><applet load="1ot5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ot5, resolution 2.40Å" /> '''The 2.4 Angstrom Cry...) |
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| - | [[Image:1ot5.gif|left|200px]]<br /><applet load="1ot5" size=" | + | [[Image:1ot5.gif|left|200px]]<br /><applet load="1ot5" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ot5, resolution 2.40Å" /> | caption="1ot5, resolution 2.40Å" /> | ||
'''The 2.4 Angstrom Crystal Sructure of Kex2 in complex with a peptidyl-boronic acid inhibitor'''<br /> | '''The 2.4 Angstrom Crystal Sructure of Kex2 in complex with a peptidyl-boronic acid inhibitor'''<br /> | ||
==Overview== | ==Overview== | ||
| - | This paper reports the first structure of a member of the Kex2/furin | + | This paper reports the first structure of a member of the Kex2/furin family of eukaryotic pro-protein processing proteases, which cleave sites consisting of pairs or clusters of basic residues. Reported is the 2.4 A resolution crystal structure of the two-domain protein ssKex2 in complex with an Ac-Ala-Lys-boroArg inhibitor (R = 20.9%, R(free) = 24.5%). The Kex2 proteolytic domain is similar in its global fold to the subtilisin-like superfamily of degradative proteases. Analysis of the complex provides a structural basis for the extreme selectivity of this enzyme family that has evolved from a nonspecific subtilisin-like ancestor. The P-domain of ssKex2 has a novel jelly roll like fold consisting of nine beta strands and may potentially be involved, along with the buried Ca(2+) ion, in creating the highly determined binding site for P(1) arginine. |
==About this Structure== | ==About this Structure== | ||
| - | 1OT5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with NAG, CA and ACE as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Kexin Kexin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.61 3.4.21.61] Full crystallographic information is available from [http:// | + | 1OT5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Kexin Kexin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.61 3.4.21.61] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OT5 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Fenn, T | + | [[Category: Fenn, T D.]] |
| - | [[Category: Fuller, R | + | [[Category: Fuller, R S.]] |
[[Category: Holyoak, T.]] | [[Category: Holyoak, T.]] | ||
| - | [[Category: Kettner, C | + | [[Category: Kettner, C A.]] |
| - | [[Category: Petsko, G | + | [[Category: Petsko, G A.]] |
[[Category: Ringe, D.]] | [[Category: Ringe, D.]] | ||
| - | [[Category: Wilson, M | + | [[Category: Wilson, M A.]] |
[[Category: ACE]] | [[Category: ACE]] | ||
[[Category: CA]] | [[Category: CA]] | ||
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[[Category: subtilisin fold]] | [[Category: subtilisin fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:21:17 2008'' |
Revision as of 12:21, 21 February 2008
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The 2.4 Angstrom Crystal Sructure of Kex2 in complex with a peptidyl-boronic acid inhibitor
Overview
This paper reports the first structure of a member of the Kex2/furin family of eukaryotic pro-protein processing proteases, which cleave sites consisting of pairs or clusters of basic residues. Reported is the 2.4 A resolution crystal structure of the two-domain protein ssKex2 in complex with an Ac-Ala-Lys-boroArg inhibitor (R = 20.9%, R(free) = 24.5%). The Kex2 proteolytic domain is similar in its global fold to the subtilisin-like superfamily of degradative proteases. Analysis of the complex provides a structural basis for the extreme selectivity of this enzyme family that has evolved from a nonspecific subtilisin-like ancestor. The P-domain of ssKex2 has a novel jelly roll like fold consisting of nine beta strands and may potentially be involved, along with the buried Ca(2+) ion, in creating the highly determined binding site for P(1) arginine.
About this Structure
1OT5 is a Single protein structure of sequence from Saccharomyces cerevisiae with , and as ligands. Active as Kexin, with EC number 3.4.21.61 Full crystallographic information is available from OCA.
Reference
2.4 A resolution crystal structure of the prototypical hormone-processing protease Kex2 in complex with an Ala-Lys-Arg boronic acid inhibitor., Holyoak T, Wilson MA, Fenn TD, Kettner CA, Petsko GA, Fuller RS, Ringe D, Biochemistry. 2003 Jun 10;42(22):6709-18. PMID:12779325
Page seeded by OCA on Thu Feb 21 14:21:17 2008
Categories: Kexin | Saccharomyces cerevisiae | Single protein | Fenn, T D. | Fuller, R S. | Holyoak, T. | Kettner, C A. | Petsko, G A. | Ringe, D. | Wilson, M A. | ACE | CA | NAG | P-domain | Peptidyl-boronic acid | Serine protease | Subtilisin fold
