1si7

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|GENE= TRUD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
|GENE= TRUD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd02575 PseudoU_synth_EcTruD], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd02552 PseudoU_synth_TruD_like], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=PRK00984 truD]</span>
|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd02575 PseudoU_synth_EcTruD], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd02552 PseudoU_synth_TruD_like], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=PRK00984 truD]</span>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1si7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1si7 OCA], [http://www.ebi.ac.uk/pdbsum/1si7 PDBsum], [http://www.fli-leibniz.de/cgi-bin/ImgLib.pl?CODE=1kfv JenaLib], [http://www.rcsb.org/pdb/explore.do?structureId=1si7 RCSB]</span>
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1si7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1si7 OCA], [http://www.ebi.ac.uk/pdbsum/1si7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1si7 RCSB]</span>
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[[Category: trud]]
[[Category: trud]]
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Revision as of 20:42, 30 March 2008


PDB ID 1si7

Drag the structure with the mouse to rotate
, resolution 2.20Å
Gene: TRUD (Escherichia coli)
Activity: Pseudouridylate synthase, with EC number 4.2.1.70
Domains: PseudoU_synth_EcTruD, PseudoU_synth_TruD_like, truD
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Structure of E. coli tRNA psi 13 pseudouridine synthase TruD


Overview

TruD, a recently discovered novel pseudouridine synthase in Escherichia coli, is responsible for modifying uridine13 in tRNA(Glu) to pseudouridine. It has little sequence homology with the other 10 pseudouridine synthases in E. coli which themselves have been grouped into four related protein families. Crystal structure determination of TruD revealed a two domain structure consisting of a catalytic domain that differs in sequence but is structurally very similar to the catalytic domain of other pseudouridine synthases and a second large domain (149 amino acids, 43% of total) with a novel alpha/beta fold that up to now has not been found in any other protein.

About this Structure

1SI7 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structure of TruD, a novel pseudouridine synthase with a new protein fold., Kaya Y, Del Campo M, Ofengand J, Malhotra A, J Biol Chem. 2004 Apr 30;279(18):18107-10. Epub 2004 Mar 3. PMID:14999002

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