Crystallization and preliminary x-ray crystallographic analysis of type II dehydroquinase from Helicobacter pylori

J. E. Kwak, J. Y. Lee, B. W. Han, J. Moon, S. H. Sohn, S. W. Suh

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

Abstract

The enzyme 3-dehydroquinase catalyzes the interconversion of 3-dehydroquinate and 3-dehydroshikimate. The enzymes are classified into two groups, type I and type II, which have different biochemical and biophysical properties and act with different mechanisms. The type II, dehydroquinase of Helicobacter pylori, a dodecameric enzyme, was overexpressed in Escherichia coli. The recombinant protein has been crystallized at 296 K using polyethylene glycol (PEG) 4000 as a precipitant. Native X-ray diffraction data have been collected to 2.5 Å resolution using synchrotron radiation. The crystals are cubic and belong to the space group P4232, with unit-cell parameters a = b = c = 98,91 Å. The asymmetric unit contains one subunit of recombinant type II dehydroquinase, with a corresponding VM of 2.18 Å3 Da-1 and a solvent content of 43.6%.

Original languageEnglish
Pages (from-to)279-280
Number of pages2
JournalActa Crystallographica Section D: Biological Crystallography
Volume57
Issue number2
DOIs
StatePublished - 2001

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