1kmm: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
|PDB= 1kmm |SIZE=350|CAPTION= <scene name='initialview01'>1kmm</scene>, resolution 2.6Å | |PDB= 1kmm |SIZE=350|CAPTION= <scene name='initialview01'>1kmm</scene>, resolution 2.6Å | ||
|SITE= <scene name='pdbsite=S1A:HIS+And+Atp+Binding+Site,+Product+Of+First+Reaction+(Int+...'>S1A</scene>, <scene name='pdbsite=S1B:HIS+And+Atp+Binding+Site,+Product+Of+First+Reaction+(Int+...'>S1B</scene>, <scene name='pdbsite=S1C:HIS+And+Atp+Binding+Site,+Product+Of+First+Reaction+(Int+...'>S1C</scene> and <scene name='pdbsite=S1D:HIS+And+Atp+Binding+Site,+Product+Of+First+Reaction+(Int+...'>S1D</scene> | |SITE= <scene name='pdbsite=S1A:HIS+And+Atp+Binding+Site,+Product+Of+First+Reaction+(Int+...'>S1A</scene>, <scene name='pdbsite=S1B:HIS+And+Atp+Binding+Site,+Product+Of+First+Reaction+(Int+...'>S1B</scene>, <scene name='pdbsite=S1C:HIS+And+Atp+Binding+Site,+Product+Of+First+Reaction+(Int+...'>S1C</scene> and <scene name='pdbsite=S1D:HIS+And+Atp+Binding+Site,+Product+Of+First+Reaction+(Int+...'>S1D</scene> | ||
|LIGAND= <scene name='pdbligand=HAM:HISTIDYL-ADENOSINE MONOPHOSPHATE'>HAM</scene> | |LIGAND= <scene name='pdbligand=HAM:HISTIDYL-ADENOSINE+MONOPHOSPHATE'>HAM</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] | |ACTIVITY= <span class='plainlinks'>[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] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kmm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kmm OCA], [http://www.ebi.ac.uk/pdbsum/1kmm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kmm RCSB]</span> | |||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Francklyn, C S.]] | [[Category: Francklyn, C S.]] | ||
[[Category: Moras, D.]] | [[Category: Moras, D.]] | ||
[[Category: aminoacyl-trna synthase]] | [[Category: aminoacyl-trna synthase]] | ||
[[Category: ligase]] | [[Category: ligase]] | ||
[[Category: synthetase]] | [[Category: synthetase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:50:38 2008'' | ||
Revision as of 21:50, 30 March 2008
| |||||||
| , resolution 2.6Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , and | ||||||
| Ligands: | |||||||
| Activity: | Histidine--tRNA ligase, with EC number 6.1.1.21 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HISTIDYL-TRNA SYNTHETASE COMPLEXED WITH HISTIDYL-ADENYLATE
OverviewOverview
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 StructureAbout this Structure
1KMM is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
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
Page seeded by OCA on Sun Mar 30 21:50:38 2008