1ctf

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==Overview==
==Overview==
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The structure of a C-terminal fragment of the ribosomal protein L7/L12, from Escherichia coli has been refined using crystallographic data to 1.7, A resolution. The R-value is 17.4%. Six residues at the N terminus are too, disordered in the structure to be localized. These residues are probably, part of a hinge in the complete L7/L12 molecule. The possibility that a, 2-fold crystallographic axis is a molecular 2-fold axis is discussed. A, patch of invariant residues on the surface of the dimer is probably, involved in functional interactions with elongation factors.
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The structure of a C-terminal fragment of the ribosomal protein L7/L12 from Escherichia coli has been refined using crystallographic data to 1.7 A resolution. The R-value is 17.4%. Six residues at the N terminus are too disordered in the structure to be localized. These residues are probably part of a hinge in the complete L7/L12 molecule. The possibility that a 2-fold crystallographic axis is a molecular 2-fold axis is discussed. A patch of invariant residues on the surface of the dimer is probably involved in functional interactions with elongation factors.
==About this Structure==
==About this Structure==
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[[Category: ribosomal protein]]
[[Category: ribosomal protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:37:06 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:09:36 2008''

Revision as of 10:09, 21 February 2008


1ctf, resolution 1.7Å

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STRUCTURE OF THE C-TERMINAL DOMAIN OF THE RIBOSOMAL PROTEIN L7/L12 FROM ESCHERICHIA COLI AT 1.7 ANGSTROMS

Overview

The structure of a C-terminal fragment of the ribosomal protein L7/L12 from Escherichia coli has been refined using crystallographic data to 1.7 A resolution. The R-value is 17.4%. Six residues at the N terminus are too disordered in the structure to be localized. These residues are probably part of a hinge in the complete L7/L12 molecule. The possibility that a 2-fold crystallographic axis is a molecular 2-fold axis is discussed. A patch of invariant residues on the surface of the dimer is probably involved in functional interactions with elongation factors.

About this Structure

1CTF is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.

Reference

Structure of the C-terminal domain of the ribosomal protein L7/L12 from Escherichia coli at 1.7 A., Leijonmarck M, Liljas A, J Mol Biol. 1987 Jun 5;195(3):555-79. PMID:3309338

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