1sry
From Proteopedia
(New page: 200px<br /><applet load="1sry" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sry, resolution 2.5Å" /> '''REFINED CRYSTAL STRUC...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1sry.gif|left|200px]]<br /><applet load="1sry" size=" | + | [[Image:1sry.gif|left|200px]]<br /><applet load="1sry" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1sry, resolution 2.5Å" /> | caption="1sry, resolution 2.5Å" /> | ||
'''REFINED CRYSTAL STRUCTURE OF THE SERYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS AT 2.5 ANGSTROMS RESOLUTION'''<br /> | '''REFINED CRYSTAL STRUCTURE OF THE SERYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS AT 2.5 ANGSTROMS RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structure of the seryl-tRNA synthetase from Thermus | + | The three-dimensional structure of the seryl-tRNA synthetase from Thermus thermophilus has been determined and refined at 2.5 A resolution. The final model consists of a dimer of 421 residues each and 190 water molecules. The R-factor is 18.4% for all the data between 10 and 2.5 A resolution. The structure is very similar to that of the homologous enzyme from Escherichia coli, with an r.m.s. difference of 1.5 A for the 357 alpha-carbon atoms considered equivalent. The comparison of the two structures indicates increased hydrophobicity, reduced conformational entropy and reduced torsional strain as possible mechanisms by which thermostability is obtained in the enzyme from the thermophile. |
==About this Structure== | ==About this Structure== | ||
| - | 1SRY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Active as [http://en.wikipedia.org/wiki/Serine--tRNA_ligase Serine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.11 6.1.1.11] Full crystallographic information is available from [http:// | + | 1SRY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Active as [http://en.wikipedia.org/wiki/Serine--tRNA_ligase Serine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.11 6.1.1.11] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SRY OCA]. |
==Reference== | ==Reference== | ||
| Line 19: | Line 19: | ||
[[Category: ligase(synthetase)]] | [[Category: ligase(synthetase)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:04:37 2008'' |
Revision as of 13:04, 21 February 2008
|
REFINED CRYSTAL STRUCTURE OF THE SERYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS AT 2.5 ANGSTROMS RESOLUTION
Overview
The three-dimensional structure of the seryl-tRNA synthetase from Thermus thermophilus has been determined and refined at 2.5 A resolution. The final model consists of a dimer of 421 residues each and 190 water molecules. The R-factor is 18.4% for all the data between 10 and 2.5 A resolution. The structure is very similar to that of the homologous enzyme from Escherichia coli, with an r.m.s. difference of 1.5 A for the 357 alpha-carbon atoms considered equivalent. The comparison of the two structures indicates increased hydrophobicity, reduced conformational entropy and reduced torsional strain as possible mechanisms by which thermostability is obtained in the enzyme from the thermophile.
About this Structure
1SRY is a Single protein structure of sequence from Thermus thermophilus. Active as Serine--tRNA ligase, with EC number 6.1.1.11 Full crystallographic information is available from OCA.
Reference
Refined crystal structure of the seryl-tRNA synthetase from Thermus thermophilus at 2.5 A resolution., Fujinaga M, Berthet-Colominas C, Yaremchuk AD, Tukalo MA, Cusack S, J Mol Biol. 1993 Nov 5;234(1):222-33. PMID:8230201
Page seeded by OCA on Thu Feb 21 15:04:37 2008
