1htt

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[[Image:1htt.gif|left|200px]]<br /><applet load="1htt" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1htt.gif|left|200px]]<br /><applet load="1htt" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1htt, resolution 2.6&Aring;" />
caption="1htt, resolution 2.6&Aring;" />
'''HISTIDYL-TRNA SYNTHETASE'''<br />
'''HISTIDYL-TRNA SYNTHETASE'''<br />
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==About this Structure==
==About this Structure==
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1HTT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with AMP as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Histidine--tRNA_ligase Histidine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.21 6.1.1.21] Known structural/functional Sites: <scene name='pdbsite=S1A:HIS And Atp Binding Sites, Product Of First Reaction (In ...'>S1A</scene>, <scene name='pdbsite=S1B:HIS And Atp Binding Sites, Product Of First Reaction (In ...'>S1B</scene>, <scene name='pdbsite=S1C:HIS And Atp Binding Sites, Product Of First Reaction (In ...'>S1C</scene> and <scene name='pdbsite=S1D:HIS And Atp Binding Sites, Product Of First Reaction (In ...'>S1D</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HTT OCA].
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1HTT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=AMP:'>AMP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Histidine--tRNA_ligase Histidine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.21 6.1.1.21] Known structural/functional Sites: <scene name='pdbsite=S1A:HIS+And+Atp+Binding+Sites,+Product+Of+First+Reaction+(In+...'>S1A</scene>, <scene name='pdbsite=S1B:HIS+And+Atp+Binding+Sites,+Product+Of+First+Reaction+(In+...'>S1B</scene>, <scene name='pdbsite=S1C:HIS+And+Atp+Binding+Sites,+Product+Of+First+Reaction+(In+...'>S1C</scene> and <scene name='pdbsite=S1D:HIS+And+Atp+Binding+Sites,+Product+Of+First+Reaction+(In+...'>S1D</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HTT OCA].
==Reference==
==Reference==
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[[Category: synthetase]]
[[Category: synthetase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 16:32:52 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:50:16 2008''

Revision as of 07:50, 3 February 2008


1htt, resolution 2.6Å

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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 with as ligand. Active as Histidine--tRNA ligase, with EC number 6.1.1.21 Known structural/functional Sites: , , and . 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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