1tfk: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
New page: left|200px<br /><applet load="1tfk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tfk, resolution 2.10Å" /> '''Ribonuclease from Es...
 
No edit summary
Line 1: Line 1:
[[Image:1tfk.gif|left|200px]]<br /><applet load="1tfk" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1tfk.gif|left|200px]]<br /><applet load="1tfk" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1tfk, resolution 2.10&Aring;" />
caption="1tfk, resolution 2.10&Aring;" />
'''Ribonuclease from Escherichia coli complexed with its inhibtor protein'''<br />
'''Ribonuclease from Escherichia coli complexed with its inhibtor protein'''<br />


==Overview==
==Overview==
Colicin D is a plasmid-encoded proteinaceous toxin which kills sensitive, Escherichia coli. Toxicity stems from ribonuclease activity that targets, exclusively four isoacceptors of tRNA(Arg) with a cleavage position, between 38 and 39 of the corresponding anticodons. Since no other tRNAs, with the same sequences at 38 and 39 as tRNA(Arg)s are cleaved, colicin D, should be capable of recognizing some higher order structure of tRNAs. We, report here two crystal structures of catalytic domains of colicin D which, have different N-terminal lengths, both complexed with its cognate, inhibitor protein, ImmD. A row of positive charge patches is found on the, surface of the catalytic domain, suggestive of the binding site of the, tRNAs. This finding, together with our refined tRNase activity, experiments, indicates that the catalytic domain starting at position 595, has activity almost equivalent to that of colicin D.
Colicin D is a plasmid-encoded proteinaceous toxin which kills sensitive Escherichia coli. Toxicity stems from ribonuclease activity that targets exclusively four isoacceptors of tRNA(Arg) with a cleavage position between 38 and 39 of the corresponding anticodons. Since no other tRNAs with the same sequences at 38 and 39 as tRNA(Arg)s are cleaved, colicin D should be capable of recognizing some higher order structure of tRNAs. We report here two crystal structures of catalytic domains of colicin D which have different N-terminal lengths, both complexed with its cognate inhibitor protein, ImmD. A row of positive charge patches is found on the surface of the catalytic domain, suggestive of the binding site of the tRNAs. This finding, together with our refined tRNase activity experiments, indicates that the catalytic domain starting at position 595 has activity almost equivalent to that of colicin D.


==About this Structure==
==About this Structure==
1TFK is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MES as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TFK OCA].  
1TFK is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MES:'>MES</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TFK OCA].  


==Reference==
==Reference==
Line 25: Line 25:
[[Category: protein-protein complex]]
[[Category: protein-protein complex]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:13:30 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:13:01 2008''

Revision as of 16:13, 21 February 2008

File:1tfk.gif


1tfk, resolution 2.10Å

Drag the structure with the mouse to rotate

Ribonuclease from Escherichia coli complexed with its inhibtor protein

OverviewOverview

Colicin D is a plasmid-encoded proteinaceous toxin which kills sensitive Escherichia coli. Toxicity stems from ribonuclease activity that targets exclusively four isoacceptors of tRNA(Arg) with a cleavage position between 38 and 39 of the corresponding anticodons. Since no other tRNAs with the same sequences at 38 and 39 as tRNA(Arg)s are cleaved, colicin D should be capable of recognizing some higher order structure of tRNAs. We report here two crystal structures of catalytic domains of colicin D which have different N-terminal lengths, both complexed with its cognate inhibitor protein, ImmD. A row of positive charge patches is found on the surface of the catalytic domain, suggestive of the binding site of the tRNAs. This finding, together with our refined tRNase activity experiments, indicates that the catalytic domain starting at position 595 has activity almost equivalent to that of colicin D.

About this StructureAbout this Structure

1TFK is a Protein complex structure of sequences from Escherichia coli with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Relation between tRNase activity and the structure of colicin D according to X-ray crystallography., Yajima S, Nakanishi K, Takahashi K, Ogawa T, Hidaka M, Kezuka Y, Nonaka T, Ohsawa K, Masaki H, Biochem Biophys Res Commun. 2004 Sep 24;322(3):966-73. PMID:15336558

Page seeded by OCA on Thu Feb 21 15:13:01 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA