2djh: Difference between revisions

Revision as of 07:08, 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:2djh.png

2djh, resolution 1.90Å ()

Ligands:

Non-Standard Residues:

Related:

2dfx

Structural annotation:
Resources:	UniProt : P18000

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

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 ribonuclease domain of Colicin E5Crystal structure of the carboxy-terminal ribonuclease domain of Colicin E5

Template:ABSTRACT PUBMED 17099236

About this StructureAbout this Structure

2DJH is a Single protein structure of sequence 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 07:08:42 2008

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

OCA

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-[[Image:2djh.gif|left|200px]]
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 {{STRUCTURE_2djh|  PDB=2djh  |  SCENE=  }}
-'''Crystal structure of the carboxy-terminal ribonuclease domain of Colicin E5'''
+===Crystal structure of the carboxy-terminal ribonuclease domain of Colicin E5===
-==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: Yajima, S.]]
 [[Category: Alpha/beta protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 00:33:13 2008''
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