2tio
From Proteopedia
(New page: 200px<br /><applet load="2tio" size="450" color="white" frame="true" align="right" spinBox="true" caption="2tio, resolution 1.93Å" /> '''LOW PACKING DENSITY ...) |
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| - | [[Image:2tio.jpg|left|200px]]<br /><applet load="2tio" size=" | + | [[Image:2tio.jpg|left|200px]]<br /><applet load="2tio" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2tio, resolution 1.93Å" /> | caption="2tio, resolution 1.93Å" /> | ||
'''LOW PACKING DENSITY FORM OF BOVINE BETA-TRYPSIN IN CYCLOHEXANE'''<br /> | '''LOW PACKING DENSITY FORM OF BOVINE BETA-TRYPSIN IN CYCLOHEXANE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Two orthorhombic forms (Vm values are 2.3 and 3.0 A3/Da) of bovine | + | Two orthorhombic forms (Vm values are 2.3 and 3.0 A3/Da) of bovine beta-trypsin crystals in neat cyclohexane were determined to 1.93 A resolution, by X-ray diffraction. Both structures in organic solvent are similar to those in aqueous solution. In the high packing density form, one cyclohexane molecule is found in a hydrophobic site near the active center. One sulfate locates at the active site with hydrogen or salt bond to the Ser-His catalytic diad, and five more sulfates bind on the molecular surface. The conformation of the side chains near the sulfates changed greatly. In the low packing density form, one cyclohexane and three sulfates are found. In both structures, one benzamidine molecule locates at the hydrophobic pocket of the active center. Most water molecules on the enzyme surface are retained except some with high temperature factors. |
==About this Structure== | ==About this Structure== | ||
| - | 2TIO 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, SO4, BEN and HEX 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:// | + | 2TIO 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>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=BEN:'>BEN</scene> and <scene name='pdbligand=HEX:'>HEX</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=2TIO OCA]. |
==Reference== | ==Reference== | ||
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[[Category: hydrolase (serine proteinase)]] | [[Category: hydrolase (serine proteinase)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:49:45 2008'' |
Revision as of 16:49, 21 February 2008
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LOW PACKING DENSITY FORM OF BOVINE BETA-TRYPSIN IN CYCLOHEXANE
Overview
Two orthorhombic forms (Vm values are 2.3 and 3.0 A3/Da) of bovine beta-trypsin crystals in neat cyclohexane were determined to 1.93 A resolution, by X-ray diffraction. Both structures in organic solvent are similar to those in aqueous solution. In the high packing density form, one cyclohexane molecule is found in a hydrophobic site near the active center. One sulfate locates at the active site with hydrogen or salt bond to the Ser-His catalytic diad, and five more sulfates bind on the molecular surface. The conformation of the side chains near the sulfates changed greatly. In the low packing density form, one cyclohexane and three sulfates are found. In both structures, one benzamidine molecule locates at the hydrophobic pocket of the active center. Most water molecules on the enzyme surface are retained except some with high temperature factors.
About this Structure
2TIO 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.
Reference
X-ray studies on two forms of bovine beta-trypsin crystals in neat cyclohexane., Zhu G, Huang Q, Wang Z, Qian M, Jia Y, Tang Y, Biochim Biophys Acta. 1998 Dec 8;1429(1):142-50. PMID:9920392
Page seeded by OCA on Thu Feb 21 18:49:45 2008
Categories: Bos taurus | Single protein | Trypsin | Huang, Q. | Tang, Q. | Zhu, G. | BEN | CA | HEX | SO4 | Benzamidine inhibited | Cyclohexane | Hydrolase (serine proteinase)
