1ob8
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(New page: 200px<br /> <applet load="1ob8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ob8, resolution 1.80Å" /> '''HOLLIDAY JUNCTION R...)
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Revision as of 15:25, 29 October 2007
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HOLLIDAY JUNCTION RESOLVING ENZYME
Overview
Two archaeal Holliday junction resolving enzymes, Holliday junction, cleavage (Hjc) and Holliday junction endonuclease (Hje), have been, characterized. Both are members of a nuclease superfamily that includes, the type II restriction enzymes, although their DNA cleaving activity is, highly specific for four-way junction structure and not nucleic acid, sequence. Despite 28% sequence identity, Hje and Hjc cleave junctions with, distinct cutting patterns--they cut different strands of a four-way, junction, at different distances from the junction centre. We report the, high-resolution crystal structure of Hje from Sulfolobus solfataricus. The, structure provides a basis to explain the differences in substrate, specificity of Hje and Hjc, which result from changes in dimer, organization, and ... [(full description)]
About this Structure
1OB8 is a [Single protein] structure of sequence from [Sulfolobus solfataricus] with SO4 and EDO as [ligands]. Full crystallographic information is available from [OCA].
Reference
Substrate recognition and catalysis by the Holliday junction resolving enzyme Hje., Middleton CL, Parker JL, Richard DJ, White MF, Bond CS, Nucleic Acids Res. 2004 Oct 12;32(18):5442-51. Print 2004. PMID:15479781
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