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1wdv
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(New page: 200px<br /><applet load="1wdv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wdv, resolution 1.70Å" /> '''Crystal structure of...)
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Revision as of 21:41, 24 November 2007
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Crystal structure of hypothetical protein APE2540
Overview
The crystal structure of APE2540, the putative trans-editing enzyme ProX, from Aeropyrum pernix K1, was determined in a high-throughput manner. The, crystal belongs to the monoclinic space group P2(1), with unit-cell, parameters a = 47.4, b = 58.9, c = 53.6 A, beta = 106.8 degrees. The, structure was solved by the multiwavelength anomalous dispersion method at, 1.7 A and refined to an R factor of 16.8% (Rfree = 20.5%). The crystal, structure includes two protein molecules in the asymmetric unit. Each, monomer consists of eight beta-strands and seven alpha-helices. A, structure-homology search revealed similarity between the trans-editing, enzyme YbaK (or cysteinyl-tRNAPro deacylase) from Haemophilus influenzae, (HI1434; 22% sequence identity) and putative ProX proteins from, Caulobacter crescentus (16%) and Agrobacterium tumefaciens (21%).
About this Structure
1WDV is a Single protein structure of sequence from Aeropyrum pernix. Full crystallographic information is available from OCA.
Reference
Structure of a putative trans-editing enzyme for prolyl-tRNA synthetase from Aeropyrum pernix K1 at 1.7 A resolution., Murayama K, Kato-Murayama M, Katsura K, Uchikubo-Kamo T, Yamaguchi-Hirafuji M, Kawazoe M, Akasaka R, Hanawa-Suetsugu K, Hori-Takemoto C, Terada T, Shirouzu M, Yokoyama S, Acta Crystallograph Sect F Struct Biol Cryst Commun. 2005 Jan 1;61(Pt, 1):26-9. Epub 2004 Dec 24. PMID:16508081
Page seeded by OCA on Sat Nov 24 23:48:35 2007
