Crystal structure of S-adenosylmethionine:tRNA ribosyltransferase-isomerase (QueA) from Thermotoga maritima at 2.0 A resolution reveals a new fold.
Mathews
Irimpan
I
Stanford Synchrotron Radiation Laboratory, Stanford University, Menlo Park, California, USA.
Schwarzenbacher
Robert
R
McMullan
Daniel
D
Abdubek
Polat
P
Ambing
Eileen
E
Axelrod
Herbert
H
Biorac
Tanya
T
Canaves
Jaume M
JM
Chiu
Hsiu-Ju
HJ
Deacon
Ashley M
AM
DiDonato
Michael
M
Elsliger
Marc-André
MA
Godzik
Adam
A
Grittini
Carina
C
Grzechnik
Slawomir K
SK
Hale
Joanna
J
Hampton
Eric
E
Han
Gye Won
GW
Haugen
Justin
J
Hornsby
Michael
M
Jaroszewski
Lukasz
L
Klock
Heath E
HE
Koesema
Eric
E
Kreusch
Andreas
A
Kuhn
Peter
P
Lesley
Scott A
SA
Levin
Inna
I
Miller
Mitchell D
MD
Moy
Kin
K
Nigoghossian
Edward
E
Ouyang
Jie
J
Paulsen
Jessica
J
Quijano
Kevin
K
Reyes
Ron
R
Spraggon
Glen
G
Stevens
Raymond C
RC
van den Bedem
Henry
H
Velasquez
Jeff
J
Vincent
Juli
J
White
Aprilfawn
A
Wolf
Guenter
G
Xu
Qingping
Q
Hodgson
Keith O
KO
Wooley
John
J
Wilson
Ian A
IA
D018360:Crystallography, X-Ray / Q000379:methods; D007535:Isomerases / Q000737:chemistry* / Q000378:metabolism; D008024:Ligands; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D012997:Solvents; D020124:Thermotoga maritima / Q000201:enzymology*
D008024:Ligands; D012997:Solvents; C082572:S-adenosylmethionine - tRNA ribosyltransferase-isomerase; D007535:Isomerases