1jrt: Difference between revisions

Revision as of 14:26, 21 February 2008

HEMIACETAL COMPLEX BETWEEN LEUPEPTIN AND TRYPSIN

OverviewOverview

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.

About this StructureAbout this Structure

1JRT is a Single protein structure of sequence from Bos taurus with and as ligands. Active as Trypsin, with EC number 3.4.21.4 Full crystallographic information is available from OCA.

ReferenceReference

Two crystal structures of the leupeptin-trypsin complex., Kurinov IV, Harrison RW, Protein Sci. 1996 Apr;5(4):752-8. PMID:8845765

Page seeded by OCA on Thu Feb 21 13:26:04 2008

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OCA

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-[[Image:1jrt.gif|left|200px]]<br /><applet load="1jrt" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1jrt.gif|left|200px]]<br /><applet load="1jrt" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1jrt, resolution 1.7&Aring;" />
 '''HEMIACETAL COMPLEX BETWEEN LEUPEPTIN AND TRYPSIN'''<br />
 ==Overview==
-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.
+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.
 ==About this Structure==
-JRT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with CA and ACE as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JRT OCA].
+JRT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JRT OCA].
 ==Reference==
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 [[Category: Single protein]]
 [[Category: Trypsin]]
-[[Category: Harrison, R.W.]]
+[[Category: Harrison, R W.]]
-[[Category: Kurinov, I.V.]]
+[[Category: Kurinov, I V.]]
 [[Category: ACE]]
 [[Category: CA]]
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 [[Category: zymogen]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:31:40 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:26:04 2008''