2pmz

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(New page: 200px<br /><applet load="2pmz" size="350" color="white" frame="true" align="right" spinBox="true" caption="2pmz, resolution 3.40&Aring;" /> '''Archaeal RNA polymer...)
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==Overview==
==Overview==
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The transcription apparatus in Archaea can be described as a simplified, version of its eukaryotic RNA polymerase (RNAP) II counterpart, comprising, an RNAPII-like enzyme as well as two general transcription factors, the, TATA-binding protein (TBP) and the eukaryotic TFIIB orthologue TFB. It has, been widely understood that precise comparisons of cellular RNAP crystal, structures could reveal structural elements common to all enzymes and that, these insights would be useful in analysing components of each enzyme that, enable it to perform domain-specific gene expression. However, the, structure of archaeal RNAP has been limited to individual subunits. Here, we report the first crystal structure of the archaeal RNAP from Sulfolobus, solfataricus at 3.4 A resolution, completing the suite of multi-subunit, RNAP structures from all three domains of life. We also report the, high-resolution (at 1.76 A) crystal structure of the D/L subcomplex of, archaeal RNAP and provide the first experimental evidence of any RNAP, possessing an iron-sulphur (Fe-S) cluster, which may play a structural, role in a key subunit of RNAP assembly. The striking structural similarity, between archaeal RNAP and eukaryotic RNAPII highlights the simpler, archaeal RNAP as an ideal model system for dissecting the molecular basis, of eukaryotic transcription.
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The transcription apparatus in Archaea can be described as a simplified version of its eukaryotic RNA polymerase (RNAP) II counterpart, comprising an RNAPII-like enzyme as well as two general transcription factors, the TATA-binding protein (TBP) and the eukaryotic TFIIB orthologue TFB. It has been widely understood that precise comparisons of cellular RNAP crystal structures could reveal structural elements common to all enzymes and that these insights would be useful in analysing components of each enzyme that enable it to perform domain-specific gene expression. However, the structure of archaeal RNAP has been limited to individual subunits. Here we report the first crystal structure of the archaeal RNAP from Sulfolobus solfataricus at 3.4 A resolution, completing the suite of multi-subunit RNAP structures from all three domains of life. We also report the high-resolution (at 1.76 A) crystal structure of the D/L subcomplex of archaeal RNAP and provide the first experimental evidence of any RNAP possessing an iron-sulphur (Fe-S) cluster, which may play a structural role in a key subunit of RNAP assembly. The striking structural similarity between archaeal RNAP and eukaryotic RNAPII highlights the simpler archaeal RNAP as an ideal model system for dissecting the molecular basis of eukaryotic transcription.
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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The X-ray crystal structure of RNA polymerase from Archaea., Hirata A, Klein BJ, Murakami KS, Nature. 2008 Jan 30;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18235446 18235446]
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The X-ray crystal structure of RNA polymerase from Archaea., Hirata A, Klein BJ, Murakami KS, Nature. 2008 Feb 14;451(7180):851-4. Epub 2008 Jan 30. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18235446 18235446]
[[Category: DNA-directed RNA polymerase]]
[[Category: DNA-directed RNA polymerase]]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Sulfolobus solfataricus]]
[[Category: Sulfolobus solfataricus]]
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[[Category: Murakami, K.S.]]
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[[Category: Murakami, K S.]]
[[Category: F3S]]
[[Category: F3S]]
[[Category: MG]]
[[Category: MG]]
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[[Category: translation]]
[[Category: translation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 13 08:20:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:31:13 2008''

Revision as of 16:31, 21 February 2008


2pmz, resolution 3.40Å

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Archaeal RNA polymerase from Sulfolobus solfataricus

Overview

The transcription apparatus in Archaea can be described as a simplified version of its eukaryotic RNA polymerase (RNAP) II counterpart, comprising an RNAPII-like enzyme as well as two general transcription factors, the TATA-binding protein (TBP) and the eukaryotic TFIIB orthologue TFB. It has been widely understood that precise comparisons of cellular RNAP crystal structures could reveal structural elements common to all enzymes and that these insights would be useful in analysing components of each enzyme that enable it to perform domain-specific gene expression. However, the structure of archaeal RNAP has been limited to individual subunits. Here we report the first crystal structure of the archaeal RNAP from Sulfolobus solfataricus at 3.4 A resolution, completing the suite of multi-subunit RNAP structures from all three domains of life. We also report the high-resolution (at 1.76 A) crystal structure of the D/L subcomplex of archaeal RNAP and provide the first experimental evidence of any RNAP possessing an iron-sulphur (Fe-S) cluster, which may play a structural role in a key subunit of RNAP assembly. The striking structural similarity between archaeal RNAP and eukaryotic RNAPII highlights the simpler archaeal RNAP as an ideal model system for dissecting the molecular basis of eukaryotic transcription.

About this Structure

2PMZ is a Protein complex structure of sequences from Sulfolobus solfataricus with , and as ligands. Active as DNA-directed RNA polymerase, with EC number 2.7.7.6 Known structural/functional Sites: , , , , , , , , , , and . Full crystallographic information is available from OCA.

Reference

The X-ray crystal structure of RNA polymerase from Archaea., Hirata A, Klein BJ, Murakami KS, Nature. 2008 Feb 14;451(7180):851-4. Epub 2008 Jan 30. PMID:18235446

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