Crystal structure of Plasmodium falciparum phosphoglycerate kinase: Evidence for anion binding in the basic patch (Q27671127)

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https://api.crossref.org/works/10.1016/J.BBRC.2011.07.045

8 December 2024

main subject

crystal structure

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Plasmodium falciparum

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phosphoglycerate kinase

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GeneDB

11 September 2018

phosphoglycerate kinase

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25 September 2018

Debasish Chattopadhyay

series ordinal

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author name string

Biswajit Pal

series ordinal

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Craig D. Smith

series ordinal

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Europe PubMed Central

PubMed publication ID

21798238

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A21798238

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language of work or name

English

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publication date

26 August 2011

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22 July 2011

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Europe PubMed Central

PubMed publication ID

21798238

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A21798238

full work available at URL

8 December 2024

https://api.elsevier.com/content/article/PII:S0006291X11012642?httpAccept=text/xml

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https://api.crossref.org/works/10.1016/J.BBRC.2011.07.045

https://api.elsevier.com/content/article/PII:S0006291X11012642?httpAccept=text/plain

8 December 2024

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Biochemical and Biophysical Research Communications

8 December 2024

published in

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volume

412

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issue

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page(s)

203-6

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A 1.8 A resolution structure of pig muscle 3-phosphoglycerate kinase with bound MgADP and 3-phosphoglycerate in open conformation: new insight into the role of the nucleotide in domain closure

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Closed structure of phosphoglycerate kinase from Thermotoga maritima reveals the catalytic mechanism and determinants of thermal stability

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A bisubstrate analog induces unexpected conformational changes in phosphoglycerate kinase from Trypanosoma brucei

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Transition state analogue structures of human phosphoglycerate kinase establish the importance of charge balance in catalysis

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Synergistic effects of substrate-induced conformational changes in phosphoglycerate kinase activation

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Crystal structures of substrates and products bound to the phosphoglycerate kinase active site reveal the catalytic mechanism

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Crystal structure of the binary complex of pig muscle phosphoglycerate kinase and its substrate 3-phospho-D-glycerate

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Site-directed mutations of arginine 65 at the periphery of the active site cleft of yeast 3-phosphoglycerate kinase enhance the catalytic activity and eliminate anion-dependent activation

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