1v7o: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
|PDB= 1v7o |SIZE=350|CAPTION= <scene name='initialview01'>1v7o</scene>, resolution 2.62Å | |PDB= 1v7o |SIZE=350|CAPTION= <scene name='initialview01'>1v7o</scene>, resolution 2.62Å | ||
|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= PH0574 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=53953 Pyrococcus horikoshii]) | |GENE= PH0574 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=53953 Pyrococcus horikoshii]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1v7o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v7o OCA], [http://www.ebi.ac.uk/pdbsum/1v7o PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1v7o RCSB]</span> | |||
}} | }} | ||
| Line 28: | Line 31: | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:20:39 2008'' | ||
Revision as of 00:20, 31 March 2008
| |||||||
| , resolution 2.62Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | PH0574 (Pyrococcus horikoshii) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Alanyl-tRNA synthetase editing domain homologue protein from Pyrococcus horikoshii
OverviewOverview
AlaX is the homologue of the class II alanyl-tRNA synthetase editing domain and has been shown to exhibit autonomous editing activity against mischarged tRNA(Ala). Here, we present the structures of AlaX from the archaeon Pyrococcus horikoshii in apo form, complexed with zinc, and with noncognate amino acid l-serine and zinc. Together with mutational analysis, we demonstrated that the conserved Thr-30 hydroxyl group located near the beta-methylene of the bound serine is responsible for the discrimination of noncognate serine from cognate alanine, based on their chemical natures. Furthermore, we confirmed that the conserved Gln-584 in alanyl-tRNA synthetase, which corresponds to Thr-30 of AlaX, is also critical for discrimination. These observations strongly suggested conservation of the chemical discrimination among trans- and cis-editing of tRNA(Ala).
About this StructureAbout this Structure
1V7O is a Single protein structure of sequence from Pyrococcus horikoshii. Full crystallographic information is available from OCA.
ReferenceReference
Molecular basis of alanine discrimination in editing site., Sokabe M, Okada A, Yao M, Nakashima T, Tanaka I, Proc Natl Acad Sci U S A. 2005 Aug 16;102(33):11669-74. Epub 2005 Aug 8. PMID:16087889
Page seeded by OCA on Mon Mar 31 00:20:39 2008