2id4

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[[Image:2id4.jpg|left|200px]]<br /><applet load="2id4" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2id4.jpg|left|200px]]
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caption="2id4, resolution 1.90&Aring;" />
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'''The 1.9 A structure of Kex2 in complex with an Ac-R-E-R-K-chloromethyl ketone inhibitor.'''<br />
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{{Structure
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|PDB= 2id4 |SIZE=350|CAPTION= <scene name='initialview01'>2id4</scene>, resolution 1.90&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> and <scene name='pdbligand=MLA:MALONIC ACID'>MLA</scene>
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|ACTIVITY= [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]
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|GENE= KEX2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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}}
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'''The 1.9 A structure of Kex2 in complex with an Ac-R-E-R-K-chloromethyl ketone inhibitor.'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2ID4 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=NA:'>NA</scene> and <scene name='pdbligand=MLA:'>MLA</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=2ID4 OCA].
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2ID4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ID4 OCA].
==Reference==
==Reference==
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Differential P1 arginine and lysine recognition in the prototypical proprotein convertase Kex2., Wheatley JL, Holyoak T, Proc Natl Acad Sci U S A. 2007 Apr 17;104(16):6626-31. Epub 2007 Apr 10. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17426142 17426142]
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Differential P1 arginine and lysine recognition in the prototypical proprotein convertase Kex2., Wheatley JL, Holyoak T, Proc Natl Acad Sci U S A. 2007 Apr 17;104(16):6626-31. Epub 2007 Apr 10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17426142 17426142]
[[Category: Kexin]]
[[Category: Kexin]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: subtilisin like protease]]
[[Category: subtilisin like protease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:51:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:28:04 2008''

Revision as of 15:28, 20 March 2008

Image:2id4.jpg


PDB ID 2id4

Drag the structure with the mouse to rotate
, resolution 1.90Å
Ligands: , , and
Gene: KEX2 (Saccharomyces cerevisiae)
Activity: Kexin, with EC number 3.4.21.61
Coordinates: save as pdb, mmCIF, xml



The 1.9 A structure of Kex2 in complex with an Ac-R-E-R-K-chloromethyl ketone inhibitor.


Overview

The high-resolution crystal structure of kexin (Kex2) in complex with a peptidyl-chloromethylketone inhibitor containing a noncognate lysine at the P(1) position provides the structural basis for the differential lysine/arginine selectivity that defines the prohormone (proprotein) convertase (PC) family. By comparison with the previous structures of Kex2 and furin, this structure of the acylated enzyme provides a basis for the observed decrease in the acylation rate with substrates containing a lysine at P(1) and the absence of an effect on the deacylation rate without involving mobility of the S(1) lid. The structure of the complex shows that a secondary subsite in the S(1) pocket is present, and that this site recognizes and binds the P(1) lysine in a more shallow fashion than arginine. This results in a displacement of the bound peptide away from the S385 nucleophile relative to substrates containing a P(1) arginine. It is concluded that this alternate binding site and resultant displacement of the scissile bond in the active site results in the observed decrease in the acylation rate. Studies of the inactivation kinetics of Kex2 by two peptidyl chloromethylketone inhibitors demonstrates that the selectivity between lysine and arginine at the P(1) position arises at the acylation step, consistent with what was observed with peptidyl substrates [Rockwell NC, Fuller RS (2001) J Biol Chem 276:38394-38399].

About this Structure

2ID4 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Differential P1 arginine and lysine recognition in the prototypical proprotein convertase Kex2., Wheatley JL, Holyoak T, Proc Natl Acad Sci U S A. 2007 Apr 17;104(16):6626-31. Epub 2007 Apr 10. PMID:17426142

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