1dmg

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(New page: 200px<br /><applet load="1dmg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dmg, resolution 1.7&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1dmg.gif|left|200px]]<br /><applet load="1dmg" size="350" color="white" frame="true" align="right" spinBox="true"
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caption="1dmg, resolution 1.7&Aring;" />
'''CRYSTAL STRUCTURE OF RIBOSOMAL PROTEIN L4'''<br />
'''CRYSTAL STRUCTURE OF RIBOSOMAL PROTEIN L4'''<br />
==Overview==
==Overview==
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Ribosomal protein L4 resides near the peptidyl transferase center of the, bacterial ribosome and may, together with rRNA and proteins L2 and L3, actively participate in the catalysis of peptide bond formation., Escherichia coli L4 is also an autogenous feedback regulator of, transcription and translation of the 11 gene S10 operon. The crystal, structure of L4 from Thermotoga maritima at 1.7 A resolution shows the, protein with an alternating alpha/beta fold and a large disordered loop, region. Two separate binding sites for RNA are discernible. The N-terminal, site, responsible for binding to rRNA, consists of the disordered loop, with flanking alpha-helices. The C-terminal site, a prime candidate for, the interaction with the leader sequence of the S10 mRNA, involves two, non-consecutive alpha-helices. The structure also suggests a C-terminal, protein-binding interface, through which L4 could be interacting with, protein components of the transcriptional and/or translational, machineries.
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Ribosomal protein L4 resides near the peptidyl transferase center of the bacterial ribosome and may, together with rRNA and proteins L2 and L3, actively participate in the catalysis of peptide bond formation. Escherichia coli L4 is also an autogenous feedback regulator of transcription and translation of the 11 gene S10 operon. The crystal structure of L4 from Thermotoga maritima at 1.7 A resolution shows the protein with an alternating alpha/beta fold and a large disordered loop region. Two separate binding sites for RNA are discernible. The N-terminal site, responsible for binding to rRNA, consists of the disordered loop with flanking alpha-helices. The C-terminal site, a prime candidate for the interaction with the leader sequence of the S10 mRNA, involves two non-consecutive alpha-helices. The structure also suggests a C-terminal protein-binding interface, through which L4 could be interacting with protein components of the transcriptional and/or translational machineries.
==About this Structure==
==About this Structure==
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1DMG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with CIT as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DMG OCA].
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1DMG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with <scene name='pdbligand=CIT:'>CIT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DMG OCA].
==Reference==
==Reference==
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[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
[[Category: Huber, R.]]
[[Category: Huber, R.]]
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[[Category: Wahl, M.C.]]
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[[Category: Wahl, M C.]]
[[Category: Worbs, M.]]
[[Category: Worbs, M.]]
[[Category: CIT]]
[[Category: CIT]]
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[[Category: s10 operon]]
[[Category: s10 operon]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:24:36 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:18:08 2008''

Revision as of 10:18, 21 February 2008

Image:1dmg.gif

1dmg, resolution 1.7Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF RIBOSOMAL PROTEIN L4

Overview

Ribosomal protein L4 resides near the peptidyl transferase center of the bacterial ribosome and may, together with rRNA and proteins L2 and L3, actively participate in the catalysis of peptide bond formation. Escherichia coli L4 is also an autogenous feedback regulator of transcription and translation of the 11 gene S10 operon. The crystal structure of L4 from Thermotoga maritima at 1.7 A resolution shows the protein with an alternating alpha/beta fold and a large disordered loop region. Two separate binding sites for RNA are discernible. The N-terminal site, responsible for binding to rRNA, consists of the disordered loop with flanking alpha-helices. The C-terminal site, a prime candidate for the interaction with the leader sequence of the S10 mRNA, involves two non-consecutive alpha-helices. The structure also suggests a C-terminal protein-binding interface, through which L4 could be interacting with protein components of the transcriptional and/or translational machineries.

About this Structure

1DMG is a Single protein structure of sequence from Thermotoga maritima with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of ribosomal protein L4 shows RNA-binding sites for ribosome incorporation and feedback control of the S10 operon., Worbs M, Huber R, Wahl MC, EMBO J. 2000 Mar 1;19(5):807-18. PMID:10698923

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