1htt
From Proteopedia
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| - | [[Image:1htt.gif|left|200px]] | + | [[Image:1htt.gif|left|200px]] |
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| - | '''HISTIDYL-TRNA SYNTHETASE''' | + | {{Structure |
| + | |PDB= 1htt |SIZE=350|CAPTION= <scene name='initialview01'>1htt</scene>, resolution 2.6Å | ||
| + | |SITE= <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> | ||
| + | |LIGAND= <scene name='pdbligand=AMP:ADENOSINE MONOPHOSPHATE'>AMP</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''HISTIDYL-TRNA SYNTHETASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HTT is a [ | + | 1HTT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HTT OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/7556055 7556055] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Histidine--tRNA ligase]] | [[Category: Histidine--tRNA ligase]] | ||
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[[Category: synthetase]] | [[Category: synthetase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:41:29 2008'' |
Revision as of 09:41, 20 March 2008
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| , resolution 2.6Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , and | ||||||
| Ligands: | |||||||
| Activity: | Histidine--tRNA ligase, with EC number 6.1.1.21 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Thu Mar 20 11:41:29 2008
