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Article: Expression, purification, crystallization and preliminary X-ray analysis of Plasmodium falciparum GTP:AMP phosphotransferase

TitleExpression, purification, crystallization and preliminary X-ray analysis of Plasmodium falciparum GTP:AMP phosphotransferase
Authors
Issue Date2012
PublisherInternational Union of Crystallography. The Journal's web site is located at http://onlinelibrary.wiley.com/journal/10.1111/%28ISSN%291744-3091
Citation
Acta Crystallographica Section F: Structural Biology and Crystallization Communications Online, 2012, F68 n. 6, p. 671–674 How to Cite?
AbstractAdenylate kinases (AKs) are phosphotransferase enzymes that catalyze the interconversion of adenine nucleotides, thereby playing an important role in energy metabolism. In Plasmodium falciparum, three AK isoforms, namely PfAK1, PfAK2 and GTP:AMP phosphotransferase (PfGAK), have been identified. While PfAK1 and PfAK2 catalyse the conversion of ATP and AMP to two molecules of ADP, PfGAK exhibits a substrate preference for GTP and AMP and does not accept ATP as a substrate. PfGAK was cloned and expressed in Escherichia coli and purified using two-step chromatography. Brown hexagonal crystals of PfGAK were obtained and a preliminary diffraction analysis was performed. X-ray diffraction data for a single PfGAK crystal were processed to 2.9 A resolution in space group P3(1)21 or P3(2)21, with unit-cell parameters a = b = 123.49, c = 180.82 A, alpha = beta = 90, gamma = 120 degrees .
Persistent Identifierhttp://hdl.handle.net/10722/149133
ISSN
2014 Impact Factor: 0.524
PubMed Central ID
ISI Accession Number ID
Funding AgencyGrant Number
HKU SPACE
Funding Information:

We would like to thank the staff at beamline 13B1 of the National Synchrotron Radiation Research Centre, Taiwan for their support and assistance. AWLL was supported by a postgraduate studentship from the HKU SPACE Research Fund.

References

 

DC FieldValueLanguage
dc.contributor.authorLaw, AWLen_HK
dc.contributor.authorLescar, Jen_HK
dc.contributor.authorHao, Qen_HK
dc.contributor.authorKotaka, Men_HK
dc.date.accessioned2012-06-22T06:25:08Z-
dc.date.available2012-06-22T06:25:08Z-
dc.date.issued2012en_HK
dc.identifier.citationActa Crystallographica Section F: Structural Biology and Crystallization Communications Online, 2012, F68 n. 6, p. 671–674en_HK
dc.identifier.issn1744-3091en_HK
dc.identifier.urihttp://hdl.handle.net/10722/149133-
dc.description.abstractAdenylate kinases (AKs) are phosphotransferase enzymes that catalyze the interconversion of adenine nucleotides, thereby playing an important role in energy metabolism. In Plasmodium falciparum, three AK isoforms, namely PfAK1, PfAK2 and GTP:AMP phosphotransferase (PfGAK), have been identified. While PfAK1 and PfAK2 catalyse the conversion of ATP and AMP to two molecules of ADP, PfGAK exhibits a substrate preference for GTP and AMP and does not accept ATP as a substrate. PfGAK was cloned and expressed in Escherichia coli and purified using two-step chromatography. Brown hexagonal crystals of PfGAK were obtained and a preliminary diffraction analysis was performed. X-ray diffraction data for a single PfGAK crystal were processed to 2.9 A resolution in space group P3(1)21 or P3(2)21, with unit-cell parameters a = b = 123.49, c = 180.82 A, alpha = beta = 90, gamma = 120 degrees .en_HK
dc.languageengen_US
dc.publisherInternational Union of Crystallography. The Journal's web site is located at http://onlinelibrary.wiley.com/journal/10.1111/%28ISSN%291744-3091en_HK
dc.relation.ispartofActa Crystallographica Section F: Structural Biology and Crystallization Communications Onlineen_HK
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.subject.meshCrystallization-
dc.subject.meshCrystallography, X-Ray-
dc.subject.meshGene Expression-
dc.subject.meshPhosphotransferases (Phosphate Group Acceptor) - chemistry - isolation and purification-
dc.subject.meshPlasmodium falciparum - enzymology-
dc.titleExpression, purification, crystallization and preliminary X-ray analysis of Plasmodium falciparum GTP:AMP phosphotransferaseen_HK
dc.typeArticleen_HK
dc.identifier.emailHao, Q: qhao@hku.hken_HK
dc.identifier.emailKotaka, M: masayo@hku.hken_HK
dc.identifier.authorityHao, Q=rp01332en_HK
dc.identifier.authorityKotaka, M=rp00293en_HK
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.1107/S1744309112015862en_HK
dc.identifier.pmid22684067-
dc.identifier.pmcidPMC3370907-
dc.identifier.scopuseid_2-s2.0-84862191498en_HK
dc.identifier.hkuros200284en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-84862191498&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volumeF68en_HK
dc.identifier.issue6en_HK
dc.identifier.spage671–674en_HK
dc.identifier.epage671–674en_HK
dc.identifier.isiWOS:000305073600014-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridKotaka, M=6604073578en_HK
dc.identifier.scopusauthoridHao, Q=7102508868en_HK
dc.identifier.scopusauthoridLescar, J=6603844493en_HK
dc.identifier.scopusauthoridLaw, AWL=55250888700en_HK
dc.identifier.citeulike10699668-

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