1kmn
From Proteopedia
(New page: 200px<br /> <applet load="1kmn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kmn, resolution 2.8Å" /> '''HISTIDYL-TRNA SYNTHE...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1KMN 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 HSO and ATP as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.21 6.1.1.21]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KMN OCA]]. | + | 1KMN 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 HSO and ATP as [[http://en.wikipedia.org/wiki/ligands ligands]]. 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=1KMN OCA]]. |
==Reference== | ==Reference== | ||
The first step of aminoacylation at the atomic level in histidyl-tRNA synthetase., Arnez JG, Augustine JG, Moras D, Francklyn CS, Proc Natl Acad Sci U S A. 1997 Jul 8;94(14):7144-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9207058 9207058] | The first step of aminoacylation at the atomic level in histidyl-tRNA synthetase., Arnez JG, Augustine JG, Moras D, Francklyn CS, Proc Natl Acad Sci U S A. 1997 Jul 8;94(14):7144-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9207058 9207058] | ||
[[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 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:27:35 2007'' |
Revision as of 11:22, 30 October 2007
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HISTIDYL-TRNA SYNTHETASE COMPLEXED WITH HISTIDINOL AND ATP
Overview
The crystal structure of an enzyme-substrate complex with histidyl-tRNA, synthetase from Escherichia coli, ATP, and the amino acid analog, histidinol is described and compared with the previously obtained, enzyme-product complex with histidyl-adenylate. An active site arginine, Arg-259, unique to all histidyl-tRNA synthetases, plays the role of the, catalytic magnesium ion seen in seryl-tRNA synthetase. When Arg-259 is, substituted with histidine, the apparent second order rate constant, (kcat/Km) for the pyrophosphate exchange reaction and the aminoacylation, reaction decreases 1,000-fold and 500-fold, respectively. Crystals soaked, with MnCl2 reveal the existence of two metal binding sites between beta-, and gamma-phosphates; these sites appear to stabilize the conformation of, the ... [(full description)]
About this Structure
1KMN is a [Single protein] structure of sequence from [Escherichia coli] with HSO and ATP as [ligands]. 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
The first step of aminoacylation at the atomic level in histidyl-tRNA synthetase., Arnez JG, Augustine JG, Moras D, Francklyn CS, Proc Natl Acad Sci U S A. 1997 Jul 8;94(14):7144-9. PMID:9207058
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