1sry

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[[Image:1sry.gif|left|200px]]
[[Image:1sry.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1sry |SIZE=350|CAPTION= <scene name='initialview01'>1sry</scene>, resolution 2.5&Aring;
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The line below this paragraph, containing "STRUCTURE_1sry", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND=
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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{{STRUCTURE_1sry| PDB=1sry | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1sry FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sry OCA], [http://www.ebi.ac.uk/pdbsum/1sry PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1sry RCSB]</span>
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}}
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'''REFINED CRYSTAL STRUCTURE OF THE SERYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS AT 2.5 ANGSTROMS RESOLUTION'''
'''REFINED CRYSTAL STRUCTURE OF THE SERYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS AT 2.5 ANGSTROMS RESOLUTION'''
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[[Category: Cusack, S.]]
[[Category: Cusack, S.]]
[[Category: Fujinaga, M.]]
[[Category: Fujinaga, M.]]
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[[Category: ligase(synthetase)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:04:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:46:11 2008''
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Revision as of 06:04, 3 May 2008

Image:1sry.gif

Template:STRUCTURE 1sry

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. 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 Sat May 3 09:04:25 2008

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