1htt
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
| - | 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/ | + | 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]]. Structure known Active Sites: S1A, S1B, S1C and S1D. Full crystallographic information is available from [[http://ispc.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://ispc.weizmann.ac.il//pmbin/getpm?pmid=7556055 7556055] | 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://ispc.weizmann.ac.il//pmbin/getpm?pmid=7556055 7556055] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| + | [[Category: Histidine--tRNA ligase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Arnez, J.G.]] | [[Category: Arnez, J.G.]] | ||
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[[Category: synthetase]] | [[Category: synthetase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:23:40 2007'' |
Revision as of 08:18, 30 October 2007
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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, ... [(full description)]
About this Structure
1HTT is a [Single protein] structure of sequence from [Escherichia coli] with AMP as [ligand]. Active as [Histidine--tRNA ligase], with EC number [6.1.1.21]. Structure known Active Sites: S1A, S1B, S1C and S1D. 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 Tue Oct 30 10:23:40 2007
