1epo
From Proteopedia
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| - | [[Image:1epo.jpg|left|200px]] | + | [[Image:1epo.jpg|left|200px]] |
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| - | '''DIRECT OBSERVATION BY X-RAY ANALYSIS OF THE TETRAHEDRAL "INTERMEDIATE" OF ASPARTIC PROTEINASES''' | + | {{Structure |
| + | |PDB= 1epo |SIZE=350|CAPTION= <scene name='initialview01'>1epo</scene>, resolution 2.0Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Endothiapepsin Endothiapepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.22 3.4.23.22] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''DIRECT OBSERVATION BY X-RAY ANALYSIS OF THE TETRAHEDRAL "INTERMEDIATE" OF ASPARTIC PROTEINASES''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1EPO is a [ | + | 1EPO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EPO OCA]. |
==Reference== | ==Reference== | ||
| - | Direct observation by X-ray analysis of the tetrahedral "intermediate" of aspartic proteinases., Veerapandian B, Cooper JB, Sali A, Blundell TL, Rosati RL, Dominy BW, Damon DB, Hoover DJ, Protein Sci. 1992 Mar;1(3):322-8. PMID:[http:// | + | Direct observation by X-ray analysis of the tetrahedral "intermediate" of aspartic proteinases., Veerapandian B, Cooper JB, Sali A, Blundell TL, Rosati RL, Dominy BW, Damon DB, Hoover DJ, Protein Sci. 1992 Mar;1(3):322-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1304340 1304340] |
[[Category: Endothiapepsin]] | [[Category: Endothiapepsin]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: hydrolase(acid proteinase)]] | [[Category: hydrolase(acid proteinase)]] | ||
| - | ''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 10:58:44 2008'' |
Revision as of 08:58, 20 March 2008
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| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Activity: | Endothiapepsin, with EC number 3.4.23.22 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
DIRECT OBSERVATION BY X-RAY ANALYSIS OF THE TETRAHEDRAL "INTERMEDIATE" OF ASPARTIC PROTEINASES
Overview
We report the X-ray analysis at 2.0 A resolution for crystals of the aspartic proteinase endothiapepsin (EC 3.4.23.6) complexed with a potent difluorostatone-containing tripeptide renin inhibitor (CP-81,282). The scissile bond surrogate, an electrophilic ketone, is hydrated in the complex. The pro-(R) (statine-like) hydroxyl of the tetrahedral carbonyl hydrate is hydrogen-bonded to both active-site aspartates 32 and 215 in the position occupied by a water in the native enzyme. The second hydroxyl oxygen of the hydrate is hydrogen-bonded only to the outer oxygen of Asp 32. These experimental data provide a basis for a model of the tetrahedral intermediate in aspartic proteinase-mediated cleavage of the amide bond. This indicates a mechanism in which Asp 32 is the proton donor and Asp 215 carboxylate polarizes a bound water for nucleophilic attack. The mechanism involves a carboxylate (Asp 32) that is stabilized by extensive hydrogen bonding, rather than an oxyanion derivative of the peptide as in serine proteinase catalysis.
About this Structure
1EPO is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Direct observation by X-ray analysis of the tetrahedral "intermediate" of aspartic proteinases., Veerapandian B, Cooper JB, Sali A, Blundell TL, Rosati RL, Dominy BW, Damon DB, Hoover DJ, Protein Sci. 1992 Mar;1(3):322-8. PMID:1304340
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