Evidence map›Paper›PMID 27487924›Full record

ArticleActa crystallographica. Section F, Structural biology communications2016

Crystallization and X-ray diffraction analysis of an L-arabinonate dehydratase from Rhizobium leguminosarum bv. trifolii and a D-xylonate dehydratase from Caulobacter crescentus.

Mohammad Mubinur Rahman, Martina Andberg, Anu Koivula, Juha Rouvinen, Nina Hakulinen

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Article in Acta crystallographica. Section F, Structural biology communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

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0cells of the map it votes in
1citing papers in PubMed
0.5field-weighted citation impact, top 31% of its field
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1 citing paper in PubMed, 4 citations in OpenAlex.

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5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Mohammad Mubinur RahmanDepartment of Chemistry, University of Eastern Finland, Joensuu Campus, PO Box 111, FIN-80101 Joensuu, Finland.
Martina AndbergVTT Technical Research Centre of Finland Ltd, PO Box 1000, FIN-02044 VTT Espoo, Finland.
Anu KoivulaVTT Technical Research Centre of Finland Ltd, PO Box 1000, FIN-02044 VTT Espoo, Finland.
Juha RouvinenDepartment of Chemistry, University of Eastern Finland, Joensuu Campus, PO Box 111, FIN-80101 Joensuu, Finland.
Nina HakulinenDepartment of Chemistry, University of Eastern Finland, Joensuu Campus, PO Box 111, FIN-80101 Joensuu, Finland.
University of Eastern Finland · FIVTT Technical Research Centre of Finland · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

L-Arabinonate dehydratase (EC 4.2.1.25) and D-xylonate dehydratase (EC 4.2.1.82) are two enzymes that are involved in a nonphosphorylative oxidation pathway of pentose sugars. L-Arabinonate dehydratase converts L-arabinonate into 2-dehydro-3-deoxy-L-arabinonate, and D-xylonate dehydratase catalyzes the dehydration of D-xylonate to 2-dehydro-3-deoxy-D-xylonate. L-Arabinonate and D-xylonate dehydratases belong to the IlvD/EDD family, together with 6-phosphogluconate dehydratases and dihydroxyacid dehydratases. No crystal structure of any L-arabinonate or D-xylonate dehydratase is available in the PDB. In this study, recombinant L-arabinonate dehydratase from Rhizobium leguminosarum bv. trifolii (RlArDHT) and D-xylonate dehydratase from Caulobacter crescentus (CcXyDHT) were heterologously expressed in Escherichia coli and purified by the use of affinity chromatography followed by gel-filtration chromatography. The purified proteins were crystallized using the hanging-drop vapour-diffusion method at 293 K. Crystals of RlArDHT that diffracted to 2.40 Å resolution were obtained using sodium formate as a precipitating agent. They belonged to space group P21, with unit-cell parameters a = 106.07, b = 208.61, c = 147.09 Å, β = 90.43°. Eight RlArDHT molecules (two tetramers) in the asymmetric unit give a VM value of 3.2 Å(3) Da(-1) and a solvent content of 62%. Crystals of CcXyDHT that diffracted to 2.66 Å resolution were obtained using sodium formate and polyethylene glycol 3350. They belonged to space group C2, with unit-cell parameters a = 270.42, b = 236.13, c = 65.17 Å, β = 97.38°. Four CcXyDHT molecules (a tetramer) in the asymmetric unit give a VM value of 4.0 Å(3) Da(-1) and a solvent content of 69%.

Indexed as

Amino Acid SequenceBacterial ProteinsCaulobacter crescentusCloning, MolecularCrystallizationCrystallography, X-RayEscherichia coliFormatesGene ExpressionHydro-LyasesPlasmidsPolyethylene GlycolsRecombinant ProteinsRhizobium leguminosarumBacterial ProteinsD-xylo-aldonate dehydrataseFormatesformic acidHydro-Lyasespolyethylene glycol 3350Polyethylene GlycolsRecombinant ProteinsCaulobacter crescentusd-xylonate dehydratase[Fe–S] clusterIlvD/EDD enzymesl-arabinonate dehydrataseRhizobium leguminosarum bv. trifolii

Identifiers

PMID27487924
PMCPMC4973301
OpenAlexW2520487465

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