1oyv: Difference between revisions

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[[Image:1oyv.jpg|left|200px]]<br /><applet load="1oyv" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1oyv.jpg|left|200px]]
caption="1oyv, resolution 2.5&Aring;" />
 
'''Crystal structure of tomato inhibitor-II in a ternary complex with subtilisin Carlsberg'''<br />
{{Structure
|PDB= 1oyv |SIZE=350|CAPTION= <scene name='initialview01'>1oyv</scene>, resolution 2.5&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
|ACTIVITY= [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]
|GENE=
}}
 
'''Crystal structure of tomato inhibitor-II in a ternary complex with subtilisin Carlsberg'''
 


==Overview==
==Overview==
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==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 <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].  
1OYV is a [[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]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OYV OCA].  


==Reference==
==Reference==
Structural basis of inhibition revealed by a 1:2 complex of the two-headed tomato inhibitor-II and subtilisin Carlsberg., Barrette-Ng IH, Ng KK, Cherney MM, Pearce G, Ryan CA, James MN, J Biol Chem. 2003 Jun 27;278(26):24062-71. Epub 2003 Apr 8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12684499 12684499]
Structural basis of inhibition revealed by a 1:2 complex of the two-headed tomato inhibitor-II and subtilisin Carlsberg., Barrette-Ng IH, Ng KK, Cherney MM, Pearce G, Ryan CA, James MN, J Biol Chem. 2003 Jun 27;278(26):24062-71. Epub 2003 Apr 8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12684499 12684499]
[[Category: Bacillus licheniformis]]
[[Category: Bacillus licheniformis]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: ternary complex]]
[[Category: ternary complex]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:23:15 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:17:32 2008''

Revision as of 14:17, 20 March 2008

File:1oyv.jpg


PDB ID 1oyv

Drag the structure with the mouse to rotate
, resolution 2.5Å
Ligands:
Activity: Subtilisin, with EC number 3.4.21.62
Coordinates: save as pdb, mmCIF, xml



Crystal structure of tomato inhibitor-II in a ternary complex with subtilisin Carlsberg


OverviewOverview

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 StructureAbout this Structure

1OYV is a Protein complex structure of sequences from Bacillus licheniformis and Solanum lycopersicum. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis of inhibition revealed by a 1:2 complex of the two-headed tomato inhibitor-II and subtilisin Carlsberg., Barrette-Ng IH, Ng KK, Cherney MM, Pearce G, Ryan CA, James MN, J Biol Chem. 2003 Jun 27;278(26):24062-71. Epub 2003 Apr 8. PMID:12684499

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