2002
DOI: 10.1074/jbc.m200481200
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Transition State Stabilization by the N-terminal Anticodon-binding Domain of Lysyl-tRNA Synthetase

Abstract: Lysyl-tRNA synthetase from Bacillus stearothermophilus (B.s. LysRS) (EC 6.1.1.6) catalyzes aminoacylation of tRNA Lys with L-lysine, in which L-lysine was first activated with ATP to yield an enzyme (lysyladenylate complex), and then the lysine molecule was transferred from the complex to tRNA Lys . B.s. LysRS is a homodimeric enzyme with a subunit that consists of two domains, an N-terminal tRNA anticodon-binding domain (TAB-ND: Ser 1 -Pro 144 ) and a C-terminal Class IIspecific catalytic domain (CAT-CD: Lys … Show more

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Cited by 10 publications
(7 citation statements)
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“…The same approach had been used earlier to characterize B . stearothermophilus LysRS active site [19]. Using the same set of analogs we investigated GenX amino acid recognition pattern (Fig.…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…The same approach had been used earlier to characterize B . stearothermophilus LysRS active site [19]. Using the same set of analogs we investigated GenX amino acid recognition pattern (Fig.…”
Section: Resultsmentioning
confidence: 99%
“…Extensive analysis of the way L-lysine analogs are recognized by E. coli LysRS has been conducted recently ( [16] and [18]). The same approach had been used earlier to characterize B. stearothermophilus LysRS active site [19]. Using the same set of analogs we investigated GenX amino acid recognition pattern (Fig.…”
Section: Genx Activates L-lysine Analogsmentioning
confidence: 99%
“…Our results show that the intact anticodon‐binding domain in wild type Ec GluRS affects transition state energetics ( k cat effect) despite being distant from the catalytic site. Isolated catalytic domain of other aaRSs, like Bacillus stearothermophilus LysRS [31] and Ec CysRS [32], also showed a much diminished catalytic activity towards their cognate aminoacylation reaction, resulting mainly from the destabilization of the transition state in the cognate amino acid activation step without affecting the ground state of substrate binding. In another report it was shown that besides being active towards cognate aminoacylation, a minimalist version of Ec GlnRS was found to charge a non‐cognate tRNA Tyr ‐derived amber suppressor ( supF ) with glutamine [33].…”
Section: Discussionmentioning
confidence: 99%
“…A naturally truncated GluRS variant (YadB), homologous to the catalytic domain, is capable of activating L‐Glu yet unable to deliver the activated Glu to either tRNA Glu or tRNA Gln [24]. A number of studies on isolated catalytic domains of other aaRSs have proved to be useful in delineating the functions of the catalytic and the anticodon‐binding domains of aaRSs [31–33]. Following this strategy we addressed the question of tRNA discrimination by studying the N‐terminal catalytic domain (NGluRS; 1–314) and the C‐terminal anticodon‐binding domain (CGluRS; 318–471) of Ec GluRS.…”
Section: Discussionmentioning
confidence: 99%
“…However, the ABDs of aaRS are diverse in structure, the ABD with a four‐helix bundle is observed in MetRS, IleRS, ValRS, LeuRS, CysRS and ArgRS [3]; the ABD of GlnRS is composed of two β‐barrel domains, but the ABDs of GluRS and LysRS‐I contain two all α‐helix domains [4]; the TyrRS_ABD comprises α + β structure; the α‐helix bundle ABD is observed at the C‐terminal of TrpRS; in ProRS, ThrRS, HisRS and glycyl‐tRNA synthetase (GlyRS), their ABDs with α/β fold structure are located at the C‐terminal; the ABDs of LysRS‐II, AspRS and AsnRS are at N‐terminal and share a β‐barrel (OB‐fold) structure [5]. The SerRS is an exceptional case, in which its N‐terminal coil domain interacts with the long variable arm of tRNA Ser , but the both anticodon loop and acceptor arm can not be recognized by SerRS [6]. It is generally believed that the primitive aaRS only contains a domain (CCD), and the ABD would be added to the N‐ or C‐terminal of CCD later; because of the ABDs’ help, the enzymes obtained the capacity to discriminate diverse tRNA specificities [7].…”
Section: Introductionmentioning
confidence: 99%