1wle
From Proteopedia
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|PDB= 1wle |SIZE=350|CAPTION= <scene name='initialview01'>1wle</scene>, resolution 1.65Å | |PDB= 1wle |SIZE=350|CAPTION= <scene name='initialview01'>1wle</scene>, resolution 1.65Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SRP:SERYL ADENYLATE'>SRP</scene> | + | |LIGAND= <scene name='pdbligand=SRP:SERYL+ADENYLATE'>SRP</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Serine--tRNA_ligase Serine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.11 6.1.1.11] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Serine--tRNA_ligase Serine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.11 6.1.1.11] </span> |
|GENE= SerRSmt ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus]) | |GENE= SerRSmt ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wle FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wle OCA], [http://www.ebi.ac.uk/pdbsum/1wle PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1wle RCSB]</span> | ||
}} | }} | ||
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[[Category: Suzuki, T.]] | [[Category: Suzuki, T.]] | ||
[[Category: Watanabe, K.]] | [[Category: Watanabe, K.]] | ||
| - | [[Category: SRP]] | ||
[[Category: ligase]] | [[Category: ligase]] | ||
| - | ''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 00:37:54 2008'' |
Revision as of 21:37, 30 March 2008
| |||||||
| , resolution 1.65Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | SerRSmt (Bos taurus) | ||||||
| Activity: | Serine--tRNA ligase, with EC number 6.1.1.11 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of mammalian mitochondrial seryl-tRNA synthetase complexed with seryl-adenylate
Overview
The secondary structures of metazoan mitochondrial (mt) tRNAs(Ser) deviate markedly from the paradigm of the canonical cloverleaf structure; particularly, tRNA(Ser)(GCU) corresponding to the AGY codon (Y=U and C) is highly truncated and intrinsically missing the entire dihydrouridine arm. None of the mt serine isoacceptors possesses the elongated variable arm, which is the universal landmark for recognition by seryl-tRNA synthetase (SerRS). Here, we report the crystal structure of mammalian mt SerRS from Bos taurus in complex with seryl adenylate at an atomic resolution of 1.65 A. Coupling structural information with a tRNA-docking model and the mutagenesis studies, we have unraveled the key elements that establish tRNA binding specificity, differ from all other known bacterial and eukaryotic systems, are the characteristic extensions in both extremities, as well as a few basic residues residing in the amino-terminal helical arm of mt SerRS. Our data further uncover an unprecedented mechanism of a dual-mode recognition employed to discriminate two distinct 'bizarre' mt tRNAs(Ser) by alternative combination of interaction sites.
About this Structure
1WLE is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Dual-mode recognition of noncanonical tRNAs(Ser) by seryl-tRNA synthetase in mammalian mitochondria., Chimnaronk S, Gravers Jeppesen M, Suzuki T, Nyborg J, Watanabe K, EMBO J. 2005 Oct 5;24(19):3369-79. Epub 2005 Sep 15. PMID:16163389
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