1si7
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(New page: 200px<br /><applet load="1si7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1si7, resolution 2.20Å" /> '''Structure of E. coli...)
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Revision as of 00:16, 21 November 2007
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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. Active as Pseudouridylate synthase, with EC number 4.2.1.70 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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