1htt: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1htt.gif|left|200px]] | [[Image:1htt.gif|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1htt", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
or leave the SCENE parameter empty for the default display. | |||
| | --> | ||
| | {{STRUCTURE_1htt| PDB=1htt | SCENE= }} | ||
}} | |||
'''HISTIDYL-TRNA SYNTHETASE''' | '''HISTIDYL-TRNA SYNTHETASE''' | ||
| Line 32: | Line 29: | ||
[[Category: Moras, D.]] | [[Category: Moras, D.]] | ||
[[Category: Rees, B.]] | [[Category: Rees, B.]] | ||
[[Category: | [[Category: Aminoacyl-trna synthase]] | ||
[[Category: | [[Category: Ligase]] | ||
[[Category: | [[Category: Synthetase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 30 13:53:14 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 10:53, 30 April 2008
HISTIDYL-TRNA SYNTHETASE
Overview
The crystal structure at 2.6 A of the histidyl-tRNA synthetase from Escherichia coli complexed with histidyl-adenylate has been determined. The enzyme is a homodimer with a molecular weight of 94 kDa and belongs to the class II of aminoacyl-tRNA synthetases (aaRS). The asymmetric unit is composed of two homodimers. Each monomer consists of two domains. The N-terminal catalytic core domain contains a six-stranded antiparallel beta-sheet sitting on two alpha-helices, which can be superposed with the catalytic domains of yeast AspRS, and GlyRS and SerRS from Thermus thermophilus with a root-mean-square difference on the C alpha atoms of 1.7-1.9 A. The active sites of all four monomers are occupied by histidyl-adenylate, which apparently forms during crystallization. The 100 residue C-terminal alpha/beta domain resembles half of a beta-barrel, and provides an independent domain oriented to contact the anticodon stem and part of the anticodon loop of tRNA(His). The modular domain organization of histidyl-tRNA synthetase reiterates a repeated theme in aaRS, and its structure should provide insight into the ability of certain aaRS to aminoacylate minihelices and other non-tRNA molecules.
About this Structure
1HTT is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of histidyl-tRNA synthetase from Escherichia coli complexed with histidyl-adenylate., Arnez JG, Harris DC, Mitschler A, Rees B, Francklyn CS, Moras D, EMBO J. 1995 Sep 1;14(17):4143-55. PMID:7556055 Page seeded by OCA on Wed Apr 30 13:53:14 2008
