1ton
From Proteopedia
(New page: 200px<br /><applet load="1ton" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ton, resolution 1.8Å" /> '''RAT SUBMAXILLARY GLAN...) |
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| - | [[Image:1ton.gif|left|200px]]<br /><applet load="1ton" size=" | + | [[Image:1ton.gif|left|200px]]<br /><applet load="1ton" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ton, resolution 1.8Å" /> | caption="1ton, resolution 1.8Å" /> | ||
'''RAT SUBMAXILLARY GLAND SERINE PROTEASE, TONIN. STRUCTURE SOLUTION AND REFINEMENT AT 1.8 ANGSTROMS RESOLUTION'''<br /> | '''RAT SUBMAXILLARY GLAND SERINE PROTEASE, TONIN. STRUCTURE SOLUTION AND REFINEMENT AT 1.8 ANGSTROMS RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Tonin is a mammalian serine protease that is capable of generating the | + | Tonin is a mammalian serine protease that is capable of generating the vasoconstrictive agent, angiotensin II, directly from its precursor protein, angiotensinogen, a process that normally requires two enzymes, renin and angiotensin-converting enzyme. The X-ray crystallographic structure determination and refinement of tonin at 1.8 A resolution and the analysis of the resulting model are reported. The initial phases were obtained by the method of molecular replacement using as the search model the structure of bovine trypsin. The refined model of tonin consists of 227 amino acid residues out of the 235 in the complete molecule, 149 water molecules, and one zinc ion. The R-factor (R = sigma Fo - Fc/sigma Fo) is 0.196 for the 14,997 measured data between 8 and 1.8 A resolution with I greater than or equal to sigma (I). It is estimated that the overall root-mean-square error in the coordinates is about 0.3 A. The structure of tonin that has been determined is not in its active conformation, but one that has been perturbed by the binding of Zn2+ in the active site. Zn2+ was included in the buffer to aid the crystallization. Nevertheless, the structure of tonin that is described is for the most part similar to its native form as indicated by the close tertiary structural homology with kallikrein. The differences in the structures of the two enzymes are concentrated in several loop regions; these structural differences are probably responsible for the differences in their reactivities and specificities. |
==About this Structure== | ==About this Structure== | ||
| - | 1TON is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1TON is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TON OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Fujinaga, M.]] | [[Category: Fujinaga, M.]] | ||
| - | [[Category: James, M | + | [[Category: James, M N.G.]] |
[[Category: ZN]] | [[Category: ZN]] | ||
[[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 15:15:46 2008'' |
Revision as of 13:15, 21 February 2008
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RAT SUBMAXILLARY GLAND SERINE PROTEASE, TONIN. STRUCTURE SOLUTION AND REFINEMENT AT 1.8 ANGSTROMS RESOLUTION
Overview
Tonin is a mammalian serine protease that is capable of generating the vasoconstrictive agent, angiotensin II, directly from its precursor protein, angiotensinogen, a process that normally requires two enzymes, renin and angiotensin-converting enzyme. The X-ray crystallographic structure determination and refinement of tonin at 1.8 A resolution and the analysis of the resulting model are reported. The initial phases were obtained by the method of molecular replacement using as the search model the structure of bovine trypsin. The refined model of tonin consists of 227 amino acid residues out of the 235 in the complete molecule, 149 water molecules, and one zinc ion. The R-factor (R = sigma Fo - Fc/sigma Fo) is 0.196 for the 14,997 measured data between 8 and 1.8 A resolution with I greater than or equal to sigma (I). It is estimated that the overall root-mean-square error in the coordinates is about 0.3 A. The structure of tonin that has been determined is not in its active conformation, but one that has been perturbed by the binding of Zn2+ in the active site. Zn2+ was included in the buffer to aid the crystallization. Nevertheless, the structure of tonin that is described is for the most part similar to its native form as indicated by the close tertiary structural homology with kallikrein. The differences in the structures of the two enzymes are concentrated in several loop regions; these structural differences are probably responsible for the differences in their reactivities and specificities.
About this Structure
1TON is a Single protein structure of sequence from Rattus rattus with as ligand. Full crystallographic information is available from OCA.
Reference
Rat submaxillary gland serine protease, tonin. Structure solution and refinement at 1.8 A resolution., Fujinaga M, James MN, J Mol Biol. 1987 May 20;195(2):373-96. PMID:2821276
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