1ais: Difference between revisions

Revision as of 12:45, 21 February 2008

TATA-BINDING PROTEIN/TRANSCRIPTION FACTOR (II)B/TATA-BOX COMPLEX FROM PYROCOCCUS WOESEI

OverviewOverview

Archaea possess a basal transcriptional apparatus that resembles that of eukaryotes. Here we report the 2.1-A crystal structure of the archaeal transcription factor complex formed by the TATA-box-binding protein (TBP), the transcription factor IIB homolog, and a DNA target, all from the hyperthermophile Pyrococcus woesei. The overall fold of these two basal transcription factors is essentially the same as that of their eukaryotic counterparts. However, in comparison with the eukaryotic complexes, the archaeal TBP-DNA interface is more symmetrical, and in this structure the orientation of the preinitiation complex assembly on the promoter is inverted with respect to that seen in all crystal structures of comparable eukaryotic systems. This study of the structural details of an archaeal transcription factor complex presents the opportunity to examine the evolution of the basal eukaryotic transcriptional apparatus from a stereochemical viewpoint and to extend our understanding of the physical biochemistry of transcriptional initiation.

About this StructureAbout this Structure

1AIS is a Protein complex structure of sequences from Pyrococcus woesei. Full crystallographic information is available from OCA.

ReferenceReference

The 2.1-A crystal structure of an archaeal preinitiation complex: TATA-box-binding protein/transcription factor (II)B core/TATA-box., Kosa PF, Ghosh G, DeDecker BS, Sigler PB, Proc Natl Acad Sci U S A. 1997 Jun 10;94(12):6042-7. PMID:9177165

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 '''TATA-BINDING PROTEIN/TRANSCRIPTION FACTOR (II)B/TATA-BOX COMPLEX FROM PYROCOCCUS WOESEI'''<br />
 ==Overview==
-Archaea possess a basal transcriptional apparatus that resembles that of, eukaryotes. Here we report the 2.1-A crystal structure of the archaeal, transcription factor complex formed by the TATA-box-binding protein (TBP), the transcription factor IIB homolog, and a DNA target, all from the, hyperthermophile Pyrococcus woesei. The overall fold of these two basal, transcription factors is essentially the same as that of their eukaryotic, counterparts. However, in comparison with the eukaryotic complexes, the, archaeal TBP-DNA interface is more symmetrical, and in this structure the, orientation of the preinitiation complex assembly on the promoter is, inverted with respect to that seen in all crystal structures of comparable, eukaryotic systems. This study of the structural details of an archaeal, transcription factor complex presents the opportunity to examine the, evolution of the basal eukaryotic transcriptional apparatus from a, stereochemical viewpoint and to extend our understanding of the physical, biochemistry of transcriptional initiation.
+Archaea possess a basal transcriptional apparatus that resembles that of eukaryotes. Here we report the 2.1-A crystal structure of the archaeal transcription factor complex formed by the TATA-box-binding protein (TBP), the transcription factor IIB homolog, and a DNA target, all from the hyperthermophile Pyrococcus woesei. The overall fold of these two basal transcription factors is essentially the same as that of their eukaryotic counterparts. However, in comparison with the eukaryotic complexes, the archaeal TBP-DNA interface is more symmetrical, and in this structure the orientation of the preinitiation complex assembly on the promoter is inverted with respect to that seen in all crystal structures of comparable eukaryotic systems. This study of the structural details of an archaeal transcription factor complex presents the opportunity to examine the evolution of the basal eukaryotic transcriptional apparatus from a stereochemical viewpoint and to extend our understanding of the physical biochemistry of transcriptional initiation.
 ==About this Structure==
-AIS is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pyrococcus_woesei Pyrococcus woesei]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AIS OCA].
+AIS is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pyrococcus_woesei Pyrococcus woesei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AIS OCA].
 ==Reference==
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 [[Category: Protein complex]]
 [[Category: Pyrococcus woesei]]
-[[Category: Dedecker, B.S.]]
+[[Category: Dedecker, B S.]]
 [[Category: Ghosh, G.]]
-[[Category: Kosa, P.F.]]
+[[Category: Kosa, P F.]]
-[[Category: Sigler, P.B.]]
+[[Category: Sigler, P B.]]
 [[Category: complex (ribosome binding/ dna)]]
 [[Category: hyperthermophile]]
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 [[Category: transcription]]
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