1bvi
From Proteopedia
(New page: 200px<br /><applet load="1bvi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bvi, resolution 1.90Å" /> '''RIBONUCLEASE T1 (WIL...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1bvi.gif|left|200px]]<br /><applet load="1bvi" size=" | + | [[Image:1bvi.gif|left|200px]]<br /><applet load="1bvi" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1bvi, resolution 1.90Å" /> | caption="1bvi, resolution 1.90Å" /> | ||
'''RIBONUCLEASE T1 (WILDTYPE) COMPLEXED WITH 2'GMP'''<br /> | '''RIBONUCLEASE T1 (WILDTYPE) COMPLEXED WITH 2'GMP'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The reoccurrence of water molecules in crystal structures of RNase T1 was | + | The reoccurrence of water molecules in crystal structures of RNase T1 was investigated. Five waters were found to be invariant in RNase T1 as well as in six other related fungal RNases. The structural, dynamical, and functional characteristics of one of these conserved hydration sites (WAT1) were analyzed by protein engineering, X-ray crystallography, and (17)O and 2H nuclear magnetic relaxation dispersion (NMRD). The position of WAT1 and its surrounding hydrogen bond network are unaffected by deletions of two neighboring side chains. In the mutant Thr93Gln, the Gln93N epsilon2 nitrogen replaces WAT1 and participates in a similar hydrogen bond network involving Cys6, Asn9, Asp76, and Thr91. The ability of WAT1 to form four hydrogen bonds may explain why evolution has preserved a water molecule, rather than a side-chain atom, at the center of this intricate hydrogen bond network. Comparison of the (17)O NMRD profiles from wild-type and Thr93Gln RNase T1 yield a mean residence time of 7 ns at 27 degrees C and an orientational order parameter of 0.45. The effects of mutations around WAT1 on the kinetic parameters of RNase T1 are small but significant and probably relate to the dynamics of the active site. |
==About this Structure== | ==About this Structure== | ||
| - | 1BVI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_oryzae Aspergillus oryzae] with CA and 2GP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ribonuclease_T(1) Ribonuclease T(1)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.3 3.1.27.3] Full crystallographic information is available from [http:// | + | 1BVI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_oryzae Aspergillus oryzae] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=2GP:'>2GP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ribonuclease_T(1) Ribonuclease T(1)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.3 3.1.27.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BVI OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Ribonuclease T(1)]] | [[Category: Ribonuclease T(1)]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Denisov, V | + | [[Category: Denisov, V P.]] |
[[Category: Doumen, J.]] | [[Category: Doumen, J.]] | ||
[[Category: Halle, B.]] | [[Category: Halle, B.]] | ||
| Line 29: | Line 29: | ||
[[Category: ribonuclease]] | [[Category: ribonuclease]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:59:34 2008'' |
Revision as of 09:59, 21 February 2008
|
RIBONUCLEASE T1 (WILDTYPE) COMPLEXED WITH 2'GMP
Overview
The reoccurrence of water molecules in crystal structures of RNase T1 was investigated. Five waters were found to be invariant in RNase T1 as well as in six other related fungal RNases. The structural, dynamical, and functional characteristics of one of these conserved hydration sites (WAT1) were analyzed by protein engineering, X-ray crystallography, and (17)O and 2H nuclear magnetic relaxation dispersion (NMRD). The position of WAT1 and its surrounding hydrogen bond network are unaffected by deletions of two neighboring side chains. In the mutant Thr93Gln, the Gln93N epsilon2 nitrogen replaces WAT1 and participates in a similar hydrogen bond network involving Cys6, Asn9, Asp76, and Thr91. The ability of WAT1 to form four hydrogen bonds may explain why evolution has preserved a water molecule, rather than a side-chain atom, at the center of this intricate hydrogen bond network. Comparison of the (17)O NMRD profiles from wild-type and Thr93Gln RNase T1 yield a mean residence time of 7 ns at 27 degrees C and an orientational order parameter of 0.45. The effects of mutations around WAT1 on the kinetic parameters of RNase T1 are small but significant and probably relate to the dynamics of the active site.
About this Structure
1BVI is a Single protein structure of sequence from Aspergillus oryzae with and as ligands. Active as Ribonuclease T(1), with EC number 3.1.27.3 Full crystallographic information is available from OCA.
Reference
Dissection of the structural and functional role of a conserved hydration site in RNase T1., Langhorst U, Loris R, Denisov VP, Doumen J, Roose P, Maes D, Halle B, Steyaert J, Protein Sci. 1999 Apr;8(4):722-30. PMID:10211818
Page seeded by OCA on Thu Feb 21 11:59:34 2008
Categories: Aspergillus oryzae | Ribonuclease T(1) | Single protein | Denisov, V P. | Doumen, J. | Halle, B. | Langhorst, U. | Loris, R. | Maes, D. | Roose, P. | Steyaert, J. | 2GP | CA | Endonuclease | Endoribonuclease | Hydrolase | Ribonuclease
