1ef4

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(New page: 200px<br /><applet load="1ef4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ef4" /> '''SOLUTION STRUCTURE OF THE ESSENTIAL RNA POLY...)
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'''SOLUTION STRUCTURE OF THE ESSENTIAL RNA POLYMERASE SUBUNIT RPB10 FROM METHANOBACTERIUM THERMOAUTOTROPHICUM'''<br />
'''SOLUTION STRUCTURE OF THE ESSENTIAL RNA POLYMERASE SUBUNIT RPB10 FROM METHANOBACTERIUM THERMOAUTOTROPHICUM'''<br />
==Overview==
==Overview==
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The RNA polymerase subunit RPB10 displays a high level of conservation, across archaea and eukarya and is required for cell viability in yeast., Structure determination of this RNA polymerase subunit from, Methanobacterium thermoautotrophicum reveals a topology, which we term a, zinc-bundle, consisting of three alpha-helices stabilized by a zinc ion., The metal ion is bound within an atypical CX(2)CX(n)CC sequence motif and, serves to bridge an N-terminal loop with helix 3. This represents an, example of two adjacent zinc-binding Cys residues within an alpha-helix, conformation. Conserved surface features of RPB10 include discrete regions, of neutral, acidic, and basic residues, the latter being located around, the zinc-binding site. One or more of these regions may contribute to the, role of this subunit as a scaffold protein within the polymerase, holoenzyme.
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The RNA polymerase subunit RPB10 displays a high level of conservation across archaea and eukarya and is required for cell viability in yeast. Structure determination of this RNA polymerase subunit from Methanobacterium thermoautotrophicum reveals a topology, which we term a zinc-bundle, consisting of three alpha-helices stabilized by a zinc ion. The metal ion is bound within an atypical CX(2)CX(n)CC sequence motif and serves to bridge an N-terminal loop with helix 3. This represents an example of two adjacent zinc-binding Cys residues within an alpha-helix conformation. Conserved surface features of RPB10 include discrete regions of neutral, acidic, and basic residues, the latter being located around the zinc-binding site. One or more of these regions may contribute to the role of this subunit as a scaffold protein within the polymerase holoenzyme.
==About this Structure==
==About this Structure==
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1EF4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/DNA-directed_RNA_polymerase DNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.6 2.7.7.6] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EF4 OCA].
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1EF4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/DNA-directed_RNA_polymerase DNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.6 2.7.7.6] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EF4 OCA].
==Reference==
==Reference==
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[[Category: Methanothermobacter thermautotrophicus]]
[[Category: Methanothermobacter thermautotrophicus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Arrowsmith, C.H.]]
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[[Category: Arrowsmith, C H.]]
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[[Category: Edwards, A.M.]]
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[[Category: Edwards, A M.]]
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[[Category: Mackereth, C.D.]]
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[[Category: Mackereth, C D.]]
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[[Category: Mcintosh, L.P.]]
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[[Category: Mcintosh, L P.]]
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[[Category: NESG, Northeast.Structural.Genomics.Consortium.]]
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[[Category: NESG, Northeast Structural Genomics Consortium.]]
[[Category: ZN]]
[[Category: ZN]]
[[Category: nesg]]
[[Category: nesg]]
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[[Category: zinc binding]]
[[Category: zinc binding]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:57:17 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:27:03 2008''

Revision as of 10:27, 21 February 2008


1ef4

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SOLUTION STRUCTURE OF THE ESSENTIAL RNA POLYMERASE SUBUNIT RPB10 FROM METHANOBACTERIUM THERMOAUTOTROPHICUM

Overview

The RNA polymerase subunit RPB10 displays a high level of conservation across archaea and eukarya and is required for cell viability in yeast. Structure determination of this RNA polymerase subunit from Methanobacterium thermoautotrophicum reveals a topology, which we term a zinc-bundle, consisting of three alpha-helices stabilized by a zinc ion. The metal ion is bound within an atypical CX(2)CX(n)CC sequence motif and serves to bridge an N-terminal loop with helix 3. This represents an example of two adjacent zinc-binding Cys residues within an alpha-helix conformation. Conserved surface features of RPB10 include discrete regions of neutral, acidic, and basic residues, the latter being located around the zinc-binding site. One or more of these regions may contribute to the role of this subunit as a scaffold protein within the polymerase holoenzyme.

About this Structure

1EF4 is a Single protein structure of sequence from Methanothermobacter thermautotrophicus with as ligand. Active as DNA-directed RNA polymerase, with EC number 2.7.7.6 Full crystallographic information is available from OCA.

Reference

Zinc-bundle structure of the essential RNA polymerase subunit RPB10 from Methanobacterium thermoautotrophicum., Mackereth CD, Arrowsmith CH, Edwards AM, McIntosh LP, Proc Natl Acad Sci U S A. 2000 Jun 6;97(12):6316-21. PMID:10841539

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