1set
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=SSA:5'-O-(N-(L-SERYL)-SULFAMOYL)ADENOSINE'>SSA</scene> | |LIGAND= <scene name='pdbligand=SSA:5'-O-(N-(L-SERYL)-SULFAMOYL)ADENOSINE'>SSA</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= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1set FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1set OCA], [http://www.ebi.ac.uk/pdbsum/1set PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1set RCSB]</span> | ||
}} | }} | ||
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[[Category: Belrhali, H.]] | [[Category: Belrhali, H.]] | ||
[[Category: Cusack, S.]] | [[Category: Cusack, S.]] | ||
| - | [[Category: SSA]] | ||
[[Category: ligase(synthetase)]] | [[Category: ligase(synthetase)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:41:04 2008'' |
Revision as of 20:41, 30 March 2008
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| , resolution 2.55Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Serine--tRNA ligase, with EC number 6.1.1.11 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURES AT 2.5 ANGSTROMS RESOLUTION OF SERYL-TRNA SYNTHETASE COMPLEXED WITH TWO DIFFERENT ANALOGUES OF SERYL-ADENYLATE
Overview
Crystal structures of seryl-tRNA synthetase from Thermus thermophilus complexed with two different analogs of seryl adenylate have been determined at 2.5 A resolution. The first complex is between the enzyme and seryl-hydroxamate-AMP (adenosine monophosphate), produced enzymatically in the crystal from adenosine triphosphate (ATP) and serine hydroxamate, and the second is with a synthetic analog of seryl adenylate (5'-O-[N-(L-seryl)-sulfamoyl]adenosine), which is a strong inhibitor of the enzyme. Both molecules are bound in a similar fashion by a network of hydrogen bond interactions in a deep hydrophilic cleft formed by the antiparallel beta sheet and surrounding loops of the synthetase catalytic domain. Four regions in the primary sequence are involved in the interactions, including the motif 2 and 3 regions of class 2 synthetases. Apart from the specific recognition of the serine side chain, the interactions are likely to be similar in all class 2 synthetases.
About this Structure
1SET is a Single protein structure of sequence from Thermus thermophilus. The following page contains interesting information on the relation of 1SET with [Aminoacyl-tRNA Synthetases]. Full crystallographic information is available from OCA.
Reference
Crystal structures at 2.5 angstrom resolution of seryl-tRNA synthetase complexed with two analogs of seryl adenylate., Belrhali H, Yaremchuk A, Tukalo M, Larsen K, Berthet-Colominas C, Leberman R, Beijer B, Sproat B, Als-Nielsen J, Grubel G, et al., Science. 1994 Mar 11;263(5152):1432-6. PMID:8128224
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