1r64
From Proteopedia
(New page: 200px<br /><applet load="1r64" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r64, resolution 2.20Å" /> '''The 2.2 A crystal st...) |
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| - | [[Image:1r64.jpg|left|200px]]<br /><applet load="1r64" size=" | + | [[Image:1r64.jpg|left|200px]]<br /><applet load="1r64" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1r64, resolution 2.20Å" /> | caption="1r64, resolution 2.20Å" /> | ||
'''The 2.2 A crystal structure of Kex2 protease in complex with Ac-Arg-Glu-Lys-boroArg peptidyl boronic acid inhibitor'''<br /> | '''The 2.2 A crystal structure of Kex2 protease in complex with Ac-Arg-Glu-Lys-boroArg peptidyl boronic acid inhibitor'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Kex2 is the yeast prototype of a large family of serine proteases that are | + | Kex2 is the yeast prototype of a large family of serine proteases that are highly specific for cleavage of their peptide substrates C-terminal to paired basic sites. This paper reports the 2.2 A resolution crystal structure of ssKex2 in complex with an Ac-Arg-Glu-Lys-Arg peptidyl boronic acid inhibitor (R = 19.7, R(free) = 23.4). By comparison of this structure with the structure of the mammalian homologue furin [Henrich, S., et al. (2003) Nat. Struct. Biol. 10, 520-526], we suggest a structural basis for the differences in substrate recognition at the P(2) and P(4) positions between Kex2 and furin and provide a structural rationale for the lack of P(6) recognition in Kex2. In addition, several monovalent cation binding sites are identified, and a mechanism of activation of Kex2 by potassium ion is proposed. |
==About this Structure== | ==About this Structure== | ||
| - | 1R64 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, K, ACE and BTB 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:// | + | 1R64 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>, <scene name='pdbligand=K:'>K</scene>, <scene name='pdbligand=ACE:'>ACE</scene> and <scene name='pdbligand=BTB:'>BTB</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=1R64 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[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: ACE]] | [[Category: ACE]] | ||
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[[Category: subtilisin]] | [[Category: subtilisin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:47:28 2008'' |
Revision as of 12:47, 21 February 2008
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The 2.2 A crystal structure of Kex2 protease in complex with Ac-Arg-Glu-Lys-boroArg peptidyl boronic acid inhibitor
Overview
Kex2 is the yeast prototype of a large family of serine proteases that are highly specific for cleavage of their peptide substrates C-terminal to paired basic sites. This paper reports the 2.2 A resolution crystal structure of ssKex2 in complex with an Ac-Arg-Glu-Lys-Arg peptidyl boronic acid inhibitor (R = 19.7, R(free) = 23.4). By comparison of this structure with the structure of the mammalian homologue furin [Henrich, S., et al. (2003) Nat. Struct. Biol. 10, 520-526], we suggest a structural basis for the differences in substrate recognition at the P(2) and P(4) positions between Kex2 and furin and provide a structural rationale for the lack of P(6) recognition in Kex2. In addition, several monovalent cation binding sites are identified, and a mechanism of activation of Kex2 by potassium ion is proposed.
About this Structure
1R64 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
Structural basis for differences in substrate selectivity in Kex2 and furin protein convertases., Holyoak T, Kettner CA, Petsko GA, Fuller RS, Ringe D, Biochemistry. 2004 Mar 9;43(9):2412-21. PMID:14992578
Page seeded by OCA on Thu Feb 21 14:47:28 2008
Categories: Kexin | Saccharomyces cerevisiae | Single protein | Fuller, R S. | Holyoak, T. | Kettner, C A. | Petsko, G A. | Ringe, D. | ACE | BTB | CA | K | NAG | Kex2 | Prohormone processing | Proprotein convertase | Protease | Protein convertase | Subtilisin
