1htt: Difference between revisions

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[[Image:1htt.gif|left|200px]]
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{{STRUCTURE_1htt|  PDB=1htt  |  SCENE=  }}  
{{STRUCTURE_1htt|  PDB=1htt  |  SCENE=  }}  


'''HISTIDYL-TRNA SYNTHETASE'''
===HISTIDYL-TRNA SYNTHETASE===




==Overview==
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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.
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{{ABSTRACT_PUBMED_7556055}}


==About this Structure==
==About this Structure==
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[[Category: Ligase]]
[[Category: Ligase]]
[[Category: Synthetase]]
[[Category: Synthetase]]
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Revision as of 05:40, 1 July 2008

File:1htt.png

Template:STRUCTURE 1htt

HISTIDYL-TRNA SYNTHETASE

Template:ABSTRACT PUBMED 7556055

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

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