1kmn

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[[Image:1kmn.gif|left|200px]]<br /><applet load="1kmn" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1kmn.gif|left|200px]]
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caption="1kmn, resolution 2.8&Aring;" />
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'''HISTIDYL-TRNA SYNTHETASE COMPLEXED WITH HISTIDINOL AND ATP'''<br />
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{{Structure
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|PDB= 1kmn |SIZE=350|CAPTION= <scene name='initialview01'>1kmn</scene>, resolution 2.8&Aring;
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|SITE= <scene name='pdbsite=S1A:HIS+And+Atp+Binding+Site,+Substrates+Of+First+Reaction+H+...'>S1A</scene>, <scene name='pdbsite=S1B:HIS+And+Atp+Binding+Site,+Substrates+Of+First+Reaction+H+...'>S1B</scene>, <scene name='pdbsite=S1C:HIS+And+Atp+Binding+Site,+Substrates+Of+First+Reaction+H+...'>S1C</scene> and <scene name='pdbsite=S1D:HIS+And+Atp+Binding+Site,+Substrates+Of+First+Reaction+H+...'>S1D</scene>
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|LIGAND= <scene name='pdbligand=HSO:HISTIDINOL'>HSO</scene> and <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene>
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|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]
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|GENE=
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}}
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'''HISTIDYL-TRNA SYNTHETASE COMPLEXED WITH HISTIDINOL AND ATP'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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 <scene name='pdbligand=HSO:'>HSO</scene> and <scene name='pdbligand=ATP:'>ATP</scene> 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] Known structural/functional Sites: <scene name='pdbsite=S1A:HIS+And+Atp+Binding+Site,+Substrates+Of+First+Reaction+H+...'>S1A</scene>, <scene name='pdbsite=S1B:HIS+And+Atp+Binding+Site,+Substrates+Of+First+Reaction+H+...'>S1B</scene>, <scene name='pdbsite=S1C:HIS+And+Atp+Binding+Site,+Substrates+Of+First+Reaction+H+...'>S1C</scene> and <scene name='pdbsite=S1D:HIS+And+Atp+Binding+Site,+Substrates+Of+First+Reaction+H+...'>S1D</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KMN OCA].
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1KMN 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=1KMN OCA].
==Reference==
==Reference==
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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]
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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://www.ncbi.nlm.nih.gov/pubmed/9207058 9207058]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Histidine--tRNA ligase]]
[[Category: Histidine--tRNA ligase]]
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[[Category: synthetase]]
[[Category: synthetase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:35:45 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:19:25 2008''

Revision as of 10:19, 20 March 2008

Image:1kmn.gif


PDB ID 1kmn

Drag the structure with the mouse to rotate
, resolution 2.8Å
Sites: , , and
Ligands: and
Activity: Histidine--tRNA ligase, with EC number 6.1.1.21
Coordinates: save as pdb, mmCIF, xml



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 pyrophosphate. The use of both conserved metal ions and arginine in phosphoryl transfer provides evidence of significant early functional divergence of class II aminoacyl-tRNA synthetases.

About this Structure

1KMN is a Single protein structure of sequence from Escherichia coli. 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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