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Title: Structure of Desulfitobacterium Hafniense PylSc, a Pyrrolysyl-TRNA Synthetase

Abstract

Pyrrolysine, the 22nd genetically-encoded amino acid, is charged onto its specific tRNA by PylS, a pyrrolysyl-tRNA synthetase. While PylS is found as a single protein in certain archaeal methanogens, in the gram-positive bacterium Desulfitobacterium hafniense, PylS is divided into two separate proteins, PylSn and PylSc, corresponding to the N-terminal and C-terminal domains of the single PylS protein found in methanogens. Previous crystallographic studies have provided the structure of a truncated C-terminal portion of the archaeal Methanosarcina mazei PylS associated with catalysis. Here, we report the apo 2.1A resolution structure of the intact D. hafniense PylSc protein and compare it to structures of the C-terminal truncated PylS from methanogenic species. In PylSc, the hydrophobic pocket binding the ring of pyrrolysine is more constrained than in the archaeal enzyme; other structural differences are also apparent.

Authors:
; ; ; ; ;
Publication Date:
Research Org.:
Stanford Linear Accelerator Center (SLAC)
Sponsoring Org.:
USDOE
OSTI Identifier:
953082
Report Number(s):
SLAC-REPRINT-2009-202
Journal ID: ISSN 0006-291X; BBRCA9; TRN: US200914%%299
DOE Contract Number:  
AC02-76SF00515
Resource Type:
Journal Article
Journal Name:
Biochem. Biophys. Res. Commun. 374:470,2008
Additional Journal Information:
Journal Volume: 374; Journal Issue: 3; Journal ID: ISSN 0006-291X
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; AMINO ACIDS; CATALYSIS; LIGASES; PROTEINS; RESOLUTION; Other,BIO, CHEM

Citation Formats

Lee, M M, Jiang, R, Jain, R, Larue, R C, Krzycki, J, and Chan, M K. Structure of Desulfitobacterium Hafniense PylSc, a Pyrrolysyl-TRNA Synthetase. United States: N. p., 2009. Web.
Lee, M M, Jiang, R, Jain, R, Larue, R C, Krzycki, J, & Chan, M K. Structure of Desulfitobacterium Hafniense PylSc, a Pyrrolysyl-TRNA Synthetase. United States.
Lee, M M, Jiang, R, Jain, R, Larue, R C, Krzycki, J, and Chan, M K. Wed . "Structure of Desulfitobacterium Hafniense PylSc, a Pyrrolysyl-TRNA Synthetase". United States.
@article{osti_953082,
title = {Structure of Desulfitobacterium Hafniense PylSc, a Pyrrolysyl-TRNA Synthetase},
author = {Lee, M M and Jiang, R and Jain, R and Larue, R C and Krzycki, J and Chan, M K},
abstractNote = {Pyrrolysine, the 22nd genetically-encoded amino acid, is charged onto its specific tRNA by PylS, a pyrrolysyl-tRNA synthetase. While PylS is found as a single protein in certain archaeal methanogens, in the gram-positive bacterium Desulfitobacterium hafniense, PylS is divided into two separate proteins, PylSn and PylSc, corresponding to the N-terminal and C-terminal domains of the single PylS protein found in methanogens. Previous crystallographic studies have provided the structure of a truncated C-terminal portion of the archaeal Methanosarcina mazei PylS associated with catalysis. Here, we report the apo 2.1A resolution structure of the intact D. hafniense PylSc protein and compare it to structures of the C-terminal truncated PylS from methanogenic species. In PylSc, the hydrophobic pocket binding the ring of pyrrolysine is more constrained than in the archaeal enzyme; other structural differences are also apparent.},
doi = {},
journal = {Biochem. Biophys. Res. Commun. 374:470,2008},
issn = {0006-291X},
number = 3,
volume = 374,
place = {United States},
year = {2009},
month = {5}
}