1a6f: Difference between revisions
New page: left|200px<br /><applet load="1a6f" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a6f, resolution 2.6Å" /> '''RNASE P PROTEIN FROM ... |
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[[Image:1a6f.gif|left|200px]]<br /><applet load="1a6f" size=" | [[Image:1a6f.gif|left|200px]]<br /><applet load="1a6f" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1a6f, resolution 2.6Å" /> | caption="1a6f, resolution 2.6Å" /> | ||
'''RNASE P PROTEIN FROM BACILLUS SUBTILIS'''<br /> | '''RNASE P PROTEIN FROM BACILLUS SUBTILIS'''<br /> | ||
==Overview== | ==Overview== | ||
The crystal structure of Bacillus subtilis ribonuclease P protein is | 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== | ||
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:// | 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]] | ||
[[Category: Christianson, D | [[Category: Christianson, D W.]] | ||
[[Category: Stams, T.]] | [[Category: Stams, T.]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
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[[Category: subunit]] | [[Category: subunit]] | ||
''Page seeded by [http:// | ''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
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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 ZN and SO4 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
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