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PMID: 17301225 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Toward understanding phosphoseryl-tRNACys formation: the crystal structure of Methanococcus maripaludis phosphoseryl-tRNA synthetase.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 104 ·No. 8 ·2007-02-20 ·Pages 2620-5

Kamtekar S, Hohn MJ, Park HS, Schnitzbauer M, Sauerwald A, Söll D, Steitz TA

Abstract

A number of archaeal organisms generate Cys-tRNA(Cys) in a two-step pathway, first charging phosphoserine (Sep) onto tRNA(Cys) and subsequently converting it to Cys-tRNA(Cys). We have determined, at 3.2-A resolution, the structure of the Methanococcus maripaludis phosphoseryl-tRNA synthetase (SepRS), which catalyzes the first step of this pathway. The structure shows that SepRS is a class II, alpha(4) synthetase whose quaternary structure arrangement of subunits closely resembles that of the heterotetrameric (alphabeta)(2) phenylalanyl-tRNA synthetase (PheRS). Homology modeling of a tRNA complex indicates that, in contrast to PheRS, a single monomer in the SepRS tetramer may recognize both the acceptor terminus and anticodon of a tRNA substrate. Using a complex with tungstate as a marker for the position of the phosphate moiety of Sep, we suggest that SepRS and PheRS bind their respective amino acid substrates in dissimilar orientations by using different residues.

MeSH Terms
Adenosine Triphosphate/metabolism Amino Acid Sequence Amino Acyl-tRNA Synthetases/chemistry Binding Sites Crystallography, X-Ray Diphosphates/metabolism Kinetics Methanococcus/chemistry,enzymology Models, Molecular Molecular Sequence Data Mutant Proteins/chemistry Phosphoserine/metabolism Protein Structure, Quaternary Protein Structure, Secondary Protein Structure, Tertiary RNA, Transfer, Cys/biosynthesis Structural Homology, Protein Thermus thermophilus/enzymology
Chemicals
Diphosphates Mutant Proteins RNA, Transfer, Cys Phosphoserine Adenosine Triphosphate Amino Acyl-tRNA Synthetases
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Kamtekar Satwik
Department of Molecular Biophysics and Biochemistry and Chemistry and Howard Hughes Medical Institute, Yale University, New Haven, CT 06520-8114, USA.
Hohn Michael J
Park Hee-Sung
Schnitzbauer Michael
Sauerwald Anselm
Söll Dieter
Steitz Thomas A
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.0611504104
Published
2007-02-20
Epub
2007-00-14
Pages
2620-5
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC1815232
Subset
IM
Grants
NIGMS NIH HHS · GM 22778 · United States
NIGMS NIH HHS · R37 GM022854 · United States
NIGMS NIH HHS · R01 GM022854 · United States
NIGMS NIH HHS · P01 GM022778 · United States
NIGMS NIH HHS · GM 22854 · United States
Databases
PDB
2ODR
External Links
PubMed source DOI: 10.1073/pnas.0611504104 PMC Full Text View journal details
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