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Article: Structural studies of glucose-6-phosphate and NADP+ binding to human glucose-6-phosphate dehydrogenase

TitleStructural studies of glucose-6-phosphate and NADP+ binding to human glucose-6-phosphate dehydrogenase
Authors
Issue Date2005
PublisherInternational Union of Crystallography. The Journal's web site is located at http://www.wiley.com/bw/editors.asp?ref=0907-4449&site=1
Citation
Acta Crystallographica Section D: Biological Crystallography, 2005, v. 61 n. 5, p. 495-504 How to Cite?
AbstractHuman glucose-6-phosphate dehydrogenase (G6PD) is NADP(+)-dependent and catalyses the first and rate-limiting step of the pentose phosphate shunt. Binary complexes of the human deletion mutant, DeltaG6PD, with glucose-6-phosphate and NADP(+) have been crystallized and their structures solved to 2.9 and 2.5 A, respectively. The structures are compared with the previously determined structure of the Canton variant of human G6PD (G6PD(Canton)) in which NADP(+) is bound at the structural site. Substrate binding in DeltaG6PD is shown to be very similar to that described previously in Leuconostoc mesenteroides G6PD. NADP(+) binding at the coenzyme site is seen to be comparable to NADP(+) binding in L. mesenteroides G6PD, although some differences arise as a result of sequence changes. The tetramer interface varies slightly among the human G6PD complexes, suggesting flexibility in the predominantly hydrophilic dimer-dimer interactions. In both complexes, Pro172 of the conserved peptide EKPxG is in the cis conformation; it is seen to be crucial for close approach of the substrate and coenzyme during the enzymatic reaction. Structural NADP(+) binds in a very similar way in the DeltaG6PD-NADP(+) complex and in G6PD(Canton), while in the substrate complex the structural NADP(+) has low occupancy and the C-terminal tail at the structural NADP(+) site is disordered. The implications of possible interaction between the structural NADP(+) and G6P are considered.
Persistent Identifierhttp://hdl.handle.net/10722/68173
ISSN
2013 Impact Factor: 7.232
2015 SCImago Journal Rankings: 3.088
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorKataka, Men_HK
dc.contributor.authorGover, Sen_HK
dc.contributor.authorVandeputte-Rutten, Sen_HK
dc.contributor.authorAu, SWNen_HK
dc.contributor.authorLam, VMSen_HK
dc.contributor.authorAdams, MJen_HK
dc.date.accessioned2010-09-06T06:02:03Z-
dc.date.available2010-09-06T06:02:03Z-
dc.date.issued2005en_HK
dc.identifier.citationActa Crystallographica Section D: Biological Crystallography, 2005, v. 61 n. 5, p. 495-504en_HK
dc.identifier.issn0907-4449en_HK
dc.identifier.urihttp://hdl.handle.net/10722/68173-
dc.description.abstractHuman glucose-6-phosphate dehydrogenase (G6PD) is NADP(+)-dependent and catalyses the first and rate-limiting step of the pentose phosphate shunt. Binary complexes of the human deletion mutant, DeltaG6PD, with glucose-6-phosphate and NADP(+) have been crystallized and their structures solved to 2.9 and 2.5 A, respectively. The structures are compared with the previously determined structure of the Canton variant of human G6PD (G6PD(Canton)) in which NADP(+) is bound at the structural site. Substrate binding in DeltaG6PD is shown to be very similar to that described previously in Leuconostoc mesenteroides G6PD. NADP(+) binding at the coenzyme site is seen to be comparable to NADP(+) binding in L. mesenteroides G6PD, although some differences arise as a result of sequence changes. The tetramer interface varies slightly among the human G6PD complexes, suggesting flexibility in the predominantly hydrophilic dimer-dimer interactions. In both complexes, Pro172 of the conserved peptide EKPxG is in the cis conformation; it is seen to be crucial for close approach of the substrate and coenzyme during the enzymatic reaction. Structural NADP(+) binds in a very similar way in the DeltaG6PD-NADP(+) complex and in G6PD(Canton), while in the substrate complex the structural NADP(+) has low occupancy and the C-terminal tail at the structural NADP(+) site is disordered. The implications of possible interaction between the structural NADP(+) and G6P are considered.en_HK
dc.languageengen_HK
dc.publisherInternational Union of Crystallography. The Journal's web site is located at http://www.wiley.com/bw/editors.asp?ref=0907-4449&site=1en_HK
dc.relation.ispartofActa Crystallographica Section D: Biological Crystallographyen_HK
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.subject.meshCrystallography, X-Ray-
dc.subject.meshEscherichia coli - chemistry - genetics-
dc.subject.meshGlucose-6-Phosphate - chemistry - metabolism-
dc.subject.meshGlucosephosphate Dehydrogenase - chemistry - genetics - metabolism-
dc.subject.meshNADP - chemistry - metabolism-
dc.titleStructural studies of glucose-6-phosphate and NADP+ binding to human glucose-6-phosphate dehydrogenaseen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=1936-0851&volume=61&spage=495&epage=504&date=2005&atitle=Structural+studies+of+glucose-6-phosphate+and+NADP++binding+to+human+glucose-6-phosphate+dehydrogenase.+en_HK
dc.identifier.emailKataka, M: masayo@hku.hken_HK
dc.identifier.emailLam, VMS: hrmbvel@hkucc.hku.hk-
dc.identifier.emailAdams, MJ: margaret.adams@biop.ox.ac.uk-
dc.identifier.authorityKotaka, M=rp00293en_HK
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.1107/S0907444905002350en_HK
dc.identifier.pmid15858258-
dc.identifier.scopuseid_2-s2.0-22844439008en_HK
dc.identifier.hkuros98967en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-22844439008&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume61en_HK
dc.identifier.issue5en_HK
dc.identifier.spage495en_HK
dc.identifier.epage504en_HK
dc.identifier.isiWOS:000228543700001-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridKotaka, M=6604073578en_HK
dc.identifier.scopusauthoridGover, S=6602155095en_HK
dc.identifier.scopusauthoridVandeputteRutten, L=6508156682en_HK
dc.identifier.scopusauthoridAu, SWN=7005457819en_HK
dc.identifier.scopusauthoridLam, VMS=7006169664en_HK
dc.identifier.scopusauthoridAdams, MJ=7403905610en_HK
dc.identifier.citeulike96326-

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