1a6f

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|PDB= 1a6f |SIZE=350|CAPTION= <scene name='initialview01'>1a6f</scene>, resolution 2.6&Aring;
|PDB= 1a6f |SIZE=350|CAPTION= <scene name='initialview01'>1a6f</scene>, resolution 2.6&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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|ACTIVITY= [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]
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|ACTIVITY= <span class='plainlinks'>[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] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a6f OCA], [http://www.ebi.ac.uk/pdbsum/1a6f PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1a6f RCSB]</span>
}}
}}
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[[Category: Christianson, D W.]]
[[Category: Christianson, D W.]]
[[Category: Stams, T.]]
[[Category: Stams, T.]]
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[[Category: SO4]]
 
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[[Category: ZN]]
 
[[Category: endonuclease]]
[[Category: endonuclease]]
[[Category: rnase]]
[[Category: rnase]]
[[Category: subunit]]
[[Category: subunit]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:53:36 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:34:15 2008''

Revision as of 15:34, 30 March 2008


PDB ID 1a6f

Drag the structure with the mouse to rotate
, resolution 2.6Å
Ligands: ,
Activity: Ribonuclease P, with EC number 3.1.26.5
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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. 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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