1SET

CRYSTAL STRUCTURES AT 2.5 ANGSTROMS RESOLUTION OF SERYL-TRNA SYNTHETASE COMPLEXED WITH TWO DIFFERENT ANALOGUES OF SERYL-ADENYLATE

Summary for 1SET

• Entry DOI: 10.2210/pdb1set/pdb
• Descriptor: SERYL-tRNA SYNTHETASE, 5'-O-(N-(L-SERYL)-SULFAMOYL)ADENOSINE (3 entities in total)
• Functional Keywords: ligase, synthetase
• Biological source: Thermus thermophilus
• Cellular location: Cytoplasm (By similarity): P34945
• Total number of polymer chains: 2
• Total formula weight: 96624.46

Authors

Cusack, S.,Belrhali, H. (deposition date: 1994-02-21, release date: 1994-07-31, Last modification date: 2024-02-14)

Primary citation

Belrhali, H.,Yaremchuk, A.,Tukalo, M.,Larsen, K.,Berthet-Colominas, C.,Leberman, R.,Beijer, B.,Sproat, B.,Als-Nielsen, J.,Grubel, G.,Legrand, J.-F.,Lehmann, M.,Cusack, S.
Crystal structures at 2.5 angstrom resolution of seryl-tRNA synthetase complexed with two analogs of seryl adenylate.
Science, 263:1432-1436, 1994

PubMed Abstract: 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.

PubMed: 8128224

Experimental method

X-RAY DIFFRACTION (2.55 Å)