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| {{STRUCTURE_1jrs| PDB=1jrs | SCENE= }} | | {{STRUCTURE_1jrs| PDB=1jrs | SCENE= }} |
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| '''HEMIACETAL COMPLEX BETWEEN LEUPEPTIN AND TRYPSIN'''
| | ===HEMIACETAL COMPLEX BETWEEN LEUPEPTIN AND TRYPSIN=== |
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| ==Overview==
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| Three-dimensional structures of trypsin with the reversible inhibitor leupeptin have been determined in two different crystal forms. The first structure was determined at 1.7 A resolution with R-factor = 17.7% in the trigonal crystal space group P3(1)21, with unit cell dimensions of a = b = 55.62 A, c = 110.51 A. The second structure was determined at a resolution of 1.8 A with R-factor = 17.5% in the orthorhombic space group P2(1)2(1)2(1), with unit cell dimensions of a = 63.69 A, b = 69.37 A, c = 63.01 A. The overall protein structure is very similar in both crystal forms, with RMS difference for main-chain atoms of 0.27 A. The leupeptin backbone forms four hydrogen bonds with trypsin and a fifth hydrogen bond interaction is mediated by a water molecule. The aldehyde carbonyl of leupeptin forms a covalent bond of 1.42 A length with side-chain oxygen of Ser-195 in the active site. The reaction of trypsin with leupeptin proceeds through the formation of stable tetrahedral complex in which the hemiacetal oxygen atom is pointing out of the oxyanion hole and forming a hydrogen bond with His-57.
| | The line below this paragraph, {{ABSTRACT_PUBMED_8845765}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 8845765 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_8845765}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Serine protease]] | | [[Category: Serine protease]] |
| [[Category: Zymogen]] | | [[Category: Zymogen]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:46:52 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:42:18 2008'' |