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1wdv

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{{STRUCTURE_1wdv| PDB=1wdv | SCENE= }}
{{STRUCTURE_1wdv| PDB=1wdv | SCENE= }}
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'''Crystal structure of hypothetical protein APE2540'''
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===Crystal structure of hypothetical protein APE2540===
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==Overview==
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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%).
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{{ABSTRACT_PUBMED_16508081}}
==About this Structure==
==About this Structure==
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[[Category: Structural genomic]]
[[Category: Structural genomic]]
[[Category: Unknown function]]
[[Category: Unknown function]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 22:59:00 2008''

Revision as of 19:59, 28 July 2008

Template:STRUCTURE 1wdv

Crystal structure of hypothetical protein APE2540

Template:ABSTRACT PUBMED 16508081

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 Crystallogr Sect F Struct Biol Cryst Commun. 2005 Jan 1;61(Pt, 1):26-9. Epub 2004 Dec 24. PMID:16508081

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