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1a6f

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(New page: 200px<br /><applet load="1a6f" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a6f, resolution 2.6&Aring;" /> '''RNASE P PROTEIN FROM ...)
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[[Image:1a6f.gif|left|200px]]<br /><applet load="1a6f" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1a6f.gif|left|200px]]<br /><applet load="1a6f" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1a6f, resolution 2.6&Aring;" />
caption="1a6f, resolution 2.6&Aring;" />
'''RNASE P PROTEIN FROM BACILLUS SUBTILIS'''<br />
'''RNASE P PROTEIN FROM BACILLUS SUBTILIS'''<br />
==Overview==
==Overview==
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The crystal structure of Bacillus subtilis ribonuclease P protein is, reported at 2.6 angstroms resolution. This protein binds to ribonuclease P, RNA to form a ribonucleoprotein holoenzyme with optimal catalytic, activity. Mutagenesis and biochemical data indicate that an unusual, left-handed betaalphabeta crossover connection and a large central cleft, in the protein form conserved RNA binding sites; a metal binding loop may, comprise a third RNA binding site. The unusual topology is partly shared, with ribosomal protein S5 and the ribosomal translocase elongation factor, G, which suggests evolution from a common RNA binding ancestor in the, primordial translational apparatus.
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The crystal structure of Bacillus subtilis ribonuclease P protein is reported at 2.6 angstroms resolution. This protein binds to ribonuclease P RNA to form a ribonucleoprotein holoenzyme with optimal catalytic activity. Mutagenesis and biochemical data indicate that an unusual left-handed betaalphabeta crossover connection and a large central cleft in the protein form conserved RNA binding sites; a metal binding loop may comprise a third RNA binding site. The unusual topology is partly shared with ribosomal protein S5 and the ribosomal translocase elongation factor G, which suggests evolution from a common RNA binding ancestor in the primordial translational apparatus.
==About this Structure==
==About this Structure==
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1A6F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with ZN and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ribonuclease_P Ribonuclease P], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.5 3.1.26.5] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A6F OCA].
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1A6F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ribonuclease_P Ribonuclease P], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.5 3.1.26.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A6F OCA].
==Reference==
==Reference==
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[[Category: Ribonuclease P]]
[[Category: Ribonuclease P]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Christianson, D.W.]]
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[[Category: Christianson, D W.]]
[[Category: Stams, T.]]
[[Category: Stams, T.]]
[[Category: SO4]]
[[Category: SO4]]
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[[Category: subunit]]
[[Category: subunit]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:38:24 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:41:35 2008''

Revision as of 09:41, 21 February 2008

Image:1a6f.gif

1a6f, resolution 2.6Å

Drag the structure with the mouse to rotate

RNASE P PROTEIN FROM BACILLUS SUBTILIS

Overview

The crystal structure of Bacillus subtilis ribonuclease P protein is reported at 2.6 angstroms resolution. This protein binds to ribonuclease P RNA to form a ribonucleoprotein holoenzyme with optimal catalytic activity. Mutagenesis and biochemical data indicate that an unusual left-handed betaalphabeta crossover connection and a large central cleft in the protein form conserved RNA binding sites; a metal binding loop may comprise a third RNA binding site. The unusual topology is partly shared with ribosomal protein S5 and the ribosomal translocase elongation factor G, which suggests evolution from a common RNA binding ancestor in the primordial translational apparatus.

About this Structure

1A6F is a Single protein structure of sequence from Bacillus subtilis with and as ligands. Active as Ribonuclease P, with EC number 3.1.26.5 Full crystallographic information is available from OCA.

Reference

Ribonuclease P protein structure: evolutionary origins in the translational apparatus., Stams T, Niranjanakumari S, Fierke CA, Christianson DW, Science. 1998 May 1;280(5364):752-5. PMID:9563955

Page seeded by OCA on Thu Feb 21 11:41:35 2008

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