TY - JOUR
T1 - Structural Basis of Transcription
T2 - Role of the Trigger Loop in Substrate Specificity and Catalysis
AU - Wang, Dong
AU - Bushnell, David A.
AU - Westover, Kenneth D.
AU - Kaplan, Craig D.
AU - Kornberg, Roger D.
N1 - Funding Information:
This research was supported by NIH grants GM49985 and GM36559 to R.D.K. C.D.K. was supported by a Fellowship from the Helen Hay Whitney Foundation. Portions of the research were carried out at the Stanford Synchrotron Radiation Laboratory, a national user facility operated by Stanford University on behalf of the U.S. Department of Energy, Office of Basic Energy Sciences. The SSRL Structural Molecular Biology Program is supported by the Department of Energy, Office of Biological and Environmental Research, and by the National Institutes of Health, National Center for Research Resources, Biomedical Technology Program, and the National Institute of General Medical Sciences. Portions of this research were conducted at the Advanced Light Source, a national user facility operated by Lawrence Berkeley National Laboratory, on behalf of the U.S. Department of Energy, Office of Basic Energy Sciences. The Berkeley Center for Structural Biology is supported in part by the Department of Energy, Office of Biological and Environmental Research, and by the National Institutes of Health, National Institute of General Medical Sciences.
PY - 2006/12/1
Y1 - 2006/12/1
N2 - New structures of RNA polymerase II (pol II) transcribing complexes reveal a likely key to transcription. The trigger loop swings beneath a correct nucleoside triphosphate (NTP) in the nucleotide addition site, closing off the active center and forming an extensive network of interactions with the NTP base, sugar, phosphates, and additional pol II residues. A histidine side chain in the trigger loop, precisely positioned by these interactions, may literally "trigger" phosphodiester bond formation. Recognition and catalysis are thus coupled, ensuring the fidelity of transcription.
AB - New structures of RNA polymerase II (pol II) transcribing complexes reveal a likely key to transcription. The trigger loop swings beneath a correct nucleoside triphosphate (NTP) in the nucleotide addition site, closing off the active center and forming an extensive network of interactions with the NTP base, sugar, phosphates, and additional pol II residues. A histidine side chain in the trigger loop, precisely positioned by these interactions, may literally "trigger" phosphodiester bond formation. Recognition and catalysis are thus coupled, ensuring the fidelity of transcription.
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U2 - 10.1016/j.cell.2006.11.023
DO - 10.1016/j.cell.2006.11.023
M3 - Article
C2 - 17129781
AN - SCOPUS:33751235874
SN - 0092-8674
VL - 127
SP - 941
EP - 954
JO - Cell
JF - Cell
IS - 5
ER -