1oyv: Difference between revisions

New page: left|200px<br /><applet load="1oyv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oyv, resolution 2.5Å" /> '''Crystal structure of ...
 
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[[Image:1oyv.jpg|left|200px]]<br /><applet load="1oyv" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1oyv.jpg|left|200px]]<br /><applet load="1oyv" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1oyv, resolution 2.5&Aring;" />
caption="1oyv, resolution 2.5&Aring;" />
'''Crystal structure of tomato inhibitor-II in a ternary complex with subtilisin Carlsberg'''<br />
'''Crystal structure of tomato inhibitor-II in a ternary complex with subtilisin Carlsberg'''<br />


==Overview==
==Overview==
Multidomain proteinase inhibitors play critical roles in the defense of, plants against predation by a wide range of pests. Despite a wealth of, structural information on proteinase-single domain inhibitor interactions, the structural basis of inhibition by multidomain proteinase inhibitors, remains poorly understood. Here we report the 2.5-A resolution crystal, structure of the two-headed tomato inhibitor-II (TI-II) in complex with, two molecules of subtilisin Carlsberg; it reveals how a multidomain, inhibitor from the Potato II family of proteinase inhibitors can bind to, and simultaneously inhibit two enzyme molecules within a single ternary, complex. The N terminus of TI-II initiates the folding of Domain I (Lys-1, to Cys-15 and Pro-84 to Met-123) and then completes Domain II (Ile-26 to, Pro-74) before coming back to complete the rest of Domain I (Pro-84 to, Met-123). The two domains of TI-II adopt a similar fold and are arranged, in an extended configuration that presents two reactive site loops at the, opposite ends of the inhibitor molecule. Each subtilisin molecule, interacts with a reactive site loop of TI-II through the standard, canonical binding mode. Remarkably, a significant distortion of the active, site of subtilisin is induced by the presence of phenylalanine in the P1, position of reactive site loop II of TI-II. The structure of the, TI-II.(subtilisin)2 complex provides a molecular framework for, understanding how multiple inhibitory domains in a single Potato II type, proteinase inhibitor molecule from the Potato II family act to inhibit, proteolytic enzymes.
Multidomain proteinase inhibitors play critical roles in the defense of plants against predation by a wide range of pests. Despite a wealth of structural information on proteinase-single domain inhibitor interactions, the structural basis of inhibition by multidomain proteinase inhibitors remains poorly understood. Here we report the 2.5-A resolution crystal structure of the two-headed tomato inhibitor-II (TI-II) in complex with two molecules of subtilisin Carlsberg; it reveals how a multidomain inhibitor from the Potato II family of proteinase inhibitors can bind to and simultaneously inhibit two enzyme molecules within a single ternary complex. The N terminus of TI-II initiates the folding of Domain I (Lys-1 to Cys-15 and Pro-84 to Met-123) and then completes Domain II (Ile-26 to Pro-74) before coming back to complete the rest of Domain I (Pro-84 to Met-123). The two domains of TI-II adopt a similar fold and are arranged in an extended configuration that presents two reactive site loops at the opposite ends of the inhibitor molecule. Each subtilisin molecule interacts with a reactive site loop of TI-II through the standard, canonical binding mode. Remarkably, a significant distortion of the active site of subtilisin is induced by the presence of phenylalanine in the P1 position of reactive site loop II of TI-II. The structure of the TI-II.(subtilisin)2 complex provides a molecular framework for understanding how multiple inhibitory domains in a single Potato II type proteinase inhibitor molecule from the Potato II family act to inhibit proteolytic enzymes.


==About this Structure==
==About this Structure==
1OYV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis] and [http://en.wikipedia.org/wiki/Solanum_lycopersicum Solanum lycopersicum] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OYV OCA].  
1OYV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis] and [http://en.wikipedia.org/wiki/Solanum_lycopersicum Solanum lycopersicum] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OYV OCA].  


==Reference==
==Reference==
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[[Category: Solanum lycopersicum]]
[[Category: Solanum lycopersicum]]
[[Category: Subtilisin]]
[[Category: Subtilisin]]
[[Category: Barrette-Ng, I.H.]]
[[Category: Barrette-Ng, I H.]]
[[Category: Cherney, M.M.]]
[[Category: Cherney, M M.]]
[[Category: James, M.N.]]
[[Category: James, M N.]]
[[Category: Ng, K.K.]]
[[Category: Ng, K K.]]
[[Category: Pearce, G.]]
[[Category: Pearce, G.]]
[[Category: Ryan, C.A.]]
[[Category: Ryan, C A.]]
[[Category: CA]]
[[Category: CA]]
[[Category: multidomain inhibitor]]
[[Category: multidomain inhibitor]]
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[[Category: ternary complex]]
[[Category: ternary complex]]


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