2dfx: Difference between revisions

Revision as of 09:29, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2dfx.png

2dfx, resolution 1.90Å ()

Related:

2djh

Structural annotation:
Resources:	UniProt : P18000, P13476

Functional annotation:
Biological process:	cytolysis defense response to bacterium bacteriocin immunity
Molecular function:	receptor binding nuclease activity endonuclease activity hydrolase activity

Evolutionary conservation:

Toggle Conservation Colors:

Rows = identical sequences:

Further Information:

Caveats,

Explanation,
Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, PDBsum, RCSB

Coordinates:

save as pdb, mmCIF, xml

Crystal structure of the carboxy terminal domain of colicin E5 complexed with its inhibitorCrystal structure of the carboxy terminal domain of colicin E5 complexed with its inhibitor

Template:ABSTRACT PUBMED 17099236

About this StructureAbout this Structure

2DFX is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for sequence-dependent recognition of colicin E5 tRNase by mimicking the mRNA-tRNA interaction., Yajima S, Inoue S, Ogawa T, Nonaka T, Ohsawa K, Masaki H, Nucleic Acids Res. 2006;34(21):6074-82. Epub 2006 Nov 11. PMID:17099236

Page seeded by OCA on Mon Jul 28 09:29:52 2008

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

OCA

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-[[Image:2dfx.gif|left|200px]]
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 {{STRUCTURE_2dfx|  PDB=2dfx  |  SCENE=  }}
-'''Crystal structure of the carboxy terminal domain of colicin E5 complexed with its inhibitor'''
+===Crystal structure of the carboxy terminal domain of colicin E5 complexed with its inhibitor===
-==Overview==
+<!--
-Colicin E5--a tRNase toxin--specifically cleaves QUN (Q: queuosine) anticodons of the Escherichia coli tRNAs for Tyr, His, Asn and Asp. Here, we report the crystal structure of the C-terminal ribonuclease domain (CRD) of E5 complexed with a substrate analog, namely, dGpdUp, at a resolution of 1.9 A. Thisstructure is the first to reveal the substrate recognition mechanism of sequence-specific ribonucleases. E5-CRD realized the strict recognition for both the guanine and uracil bases of dGpdUp forming Watson-Crick-type hydrogen bonds and ring stacking interactions, thus mimicking the codons of mRNAs to bind to tRNA anticodons. The docking model of E5-CRD with tRNA also suggests its substrate preference for tRNA over ssRNA. In addition, the structure of E5-CRD/dGpdUp along with the mutational analysis suggests that Arg33 may play an important role in the catalytic activity, and Lys25/Lys60 may also be involved without His in E5-CRD. Finally, the comparison of the structures of E5-CRD/dGpdUp and E5-CRD/ImmE5 (an inhibitor protein) complexes suggests that the binding mode of E5-CRD and ImmE5 mimics that of mRNA and tRNA; this may represent the evolutionary pathway of these proteins from the RNA-RNA interaction through the RNA-protein interaction of tRNA/E5-CRD.
+The line below this paragraph, {{ABSTRACT_PUBMED_17099236}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17099236 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17099236}}
 ==About this Structure==
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 [[Category: Alpha/beta protein]]
 [[Category: Protein-inhibitor protein complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 00:20:33 2008''
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