1dp5: Difference between revisions
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[[Image:1dp5.gif|left|200px]] | [[Image:1dp5.gif|left|200px]] | ||
'''THE STRUCTURE OF PROTEINASE A COMPLEXED WITH A IA3 MUTANT INHIBITOR''' | {{Structure | ||
|PDB= 1dp5 |SIZE=350|CAPTION= <scene name='initialview01'>1dp5</scene>, resolution 2.2Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Saccharopepsin Saccharopepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.25 3.4.23.25] | |||
|GENE= | |||
}} | |||
'''THE STRUCTURE OF PROTEINASE A COMPLEXED WITH A IA3 MUTANT INHIBITOR''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1DP5 is a [ | 1DP5 is a [[Protein complex]] structure of sequences 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=1DP5 OCA]. | ||
==Reference== | ==Reference== | ||
The aspartic proteinase from Saccharomyces cerevisiae folds its own inhibitor into a helix., Li M, Phylip LH, Lees WE, Winther JR, Dunn BM, Wlodawer A, Kay J, Gustchina A, Nat Struct Biol. 2000 Feb;7(2):113-7. PMID:[http:// | The aspartic proteinase from Saccharomyces cerevisiae folds its own inhibitor into a helix., Li M, Phylip LH, Lees WE, Winther JR, Dunn BM, Wlodawer A, Kay J, Gustchina A, Nat Struct Biol. 2000 Feb;7(2):113-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10655612 10655612] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
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[[Category: ia3 mutant]] | [[Category: ia3 mutant]] | ||
[[Category: mmm]] | [[Category: mmm]] | ||
[[Category: proteinase | [[Category: proteinase some]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:42:00 2008'' | ||
Revision as of 11:42, 20 March 2008
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| , resolution 2.2Å | |||||||
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| Activity: | Saccharopepsin, with EC number 3.4.23.25 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE STRUCTURE OF PROTEINASE A COMPLEXED WITH A IA3 MUTANT INHIBITOR
OverviewOverview
Aspartic proteinase A from yeast is specifically and potently inhibited by a small protein called IA3 from Saccharomyces cerevisiae. Although this inhibitor consists of 68 residues, we show that the inhibitory activity resides within the N-terminal half of the molecule. Structures solved at 2.2 and 1.8 A, respectively, for complexes of proteinase A with full-length IA3 and with a truncated form consisting only of residues 2-34, reveal an unprecedented mode of inhibitor-enzyme interactions. Neither form of the free inhibitor has detectable intrinsic secondary structure in solution. However, upon contact with the enzyme, residues 2-32 become ordered and adopt a near-perfect alpha-helical conformation. Thus, the proteinase acts as a folding template, stabilizing the helical conformation in the inhibitor, which results in the potent and specific blockage of the proteolytic activity.
About this StructureAbout this Structure
1DP5 is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
The aspartic proteinase from Saccharomyces cerevisiae folds its own inhibitor into a helix., Li M, Phylip LH, Lees WE, Winther JR, Dunn BM, Wlodawer A, Kay J, Gustchina A, Nat Struct Biol. 2000 Feb;7(2):113-7. PMID:10655612
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