1grj

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(New page: 200px<br /><applet load="1grj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1grj, resolution 2.2&Aring;" /> '''GREA TRANSCRIPT CLEAV...)
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caption="1grj, resolution 2.2&Aring;" />
'''GREA TRANSCRIPT CLEAVAGE FACTOR FROM ESCHERICHIA COLI'''<br />
'''GREA TRANSCRIPT CLEAVAGE FACTOR FROM ESCHERICHIA COLI'''<br />
==Overview==
==Overview==
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Transcription elongation factors stimulate the activity of DNA-dependent, RNA polymerases by increasing the overall elongation rate and the, completion of RNA chains. One group of such factors, which includes, Escherichia coli GreA, GreB and eukaryotic SII (TFIIS), acts by inducing, hydrolytic cleavage of the transcript within the RNA polymerase, followed, by release of the 3'-terminal fragment. Here we report the crystal, structure of GreA at 2.2 A resolution. The structure contains an, amino-terminal domain consisting of an antiparallel alpha-helical, coiled-coil dimer which extends into solution, reminiscent of the coiled, coil in seryl-tRNA synthetases. A site near the tip of the coiled-coil, 'finger' plays a direct role in the transcript cleavage reaction by, contacting the 3'-end of the transcript. The structure exhibits an unusual, asymmetric charge distribution which indicates the manner in which GreA, interacts with the RNA polymerase elongation complex.
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Transcription elongation factors stimulate the activity of DNA-dependent RNA polymerases by increasing the overall elongation rate and the completion of RNA chains. One group of such factors, which includes Escherichia coli GreA, GreB and eukaryotic SII (TFIIS), acts by inducing hydrolytic cleavage of the transcript within the RNA polymerase, followed by release of the 3'-terminal fragment. Here we report the crystal structure of GreA at 2.2 A resolution. The structure contains an amino-terminal domain consisting of an antiparallel alpha-helical coiled-coil dimer which extends into solution, reminiscent of the coiled coil in seryl-tRNA synthetases. A site near the tip of the coiled-coil 'finger' plays a direct role in the transcript cleavage reaction by contacting the 3'-end of the transcript. The structure exhibits an unusual asymmetric charge distribution which indicates the manner in which GreA interacts with the RNA polymerase elongation complex.
==About this Structure==
==About this Structure==
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1GRJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GRJ OCA].
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1GRJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GRJ OCA].
==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Darst, S.A.]]
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[[Category: Darst, S A.]]
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[[Category: Stebbins, C.E.]]
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[[Category: Stebbins, C E.]]
[[Category: transcript cleavage factor]]
[[Category: transcript cleavage factor]]
[[Category: transcript elongation factor]]
[[Category: transcript elongation factor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:15:03 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:53:11 2008''

Revision as of 10:53, 21 February 2008

Image:1grj.jpg

1grj, resolution 2.2Å

Drag the structure with the mouse to rotate

GREA TRANSCRIPT CLEAVAGE FACTOR FROM ESCHERICHIA COLI

Overview

Transcription elongation factors stimulate the activity of DNA-dependent RNA polymerases by increasing the overall elongation rate and the completion of RNA chains. One group of such factors, which includes Escherichia coli GreA, GreB and eukaryotic SII (TFIIS), acts by inducing hydrolytic cleavage of the transcript within the RNA polymerase, followed by release of the 3'-terminal fragment. Here we report the crystal structure of GreA at 2.2 A resolution. The structure contains an amino-terminal domain consisting of an antiparallel alpha-helical coiled-coil dimer which extends into solution, reminiscent of the coiled coil in seryl-tRNA synthetases. A site near the tip of the coiled-coil 'finger' plays a direct role in the transcript cleavage reaction by contacting the 3'-end of the transcript. The structure exhibits an unusual asymmetric charge distribution which indicates the manner in which GreA interacts with the RNA polymerase elongation complex.

About this Structure

1GRJ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structure of the GreA transcript cleavage factor from Escherichia coli., Stebbins CE, Borukhov S, Orlova M, Polyakov A, Goldfarb A, Darst SA, Nature. 1995 Feb 16;373(6515):636-40. PMID:7854424

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