Hauptseite > Publikationsdatenbank > A Spring Loaded Release Mechanism Regulates Domain Movement and Catalysis in Phosphoglycerate Kinase. > print

001     16685
005     20200402210045.0
024 7 _ |2 pmid
|a pmid:21349853
024 7 _ |2 pmc
|a pmc:PMC3077604
024 7 _ |2 DOI
|a 10.1074/jbc.M110.206813
024 7 _ |2 WOS
|a WOS:000289556200026
024 7 _ |a altmetric:3373743
|2 altmetric
037 _ _ |a PreJuSER-16685
041 _ _ |a eng
082 _ _ |a 570
084 _ _ |2 WoS
|a Biochemistry & Molecular Biology
100 1 _ |0 P:(DE-Juel1)VDB101251
|a Zerrad, L.
|b 0
|u FZJ
245 _ _ |a A Spring Loaded Release Mechanism Regulates Domain Movement and Catalysis in Phosphoglycerate Kinase.
260 _ _ |a Bethesda, Md.
|b Soc.
|c 2011
300 _ _ |a 14040 - 14048
336 7 _ |a Journal Article
|0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
336 7 _ |a Output Types/Journal article
|2 DataCite
336 7 _ |a Journal Article
|0 0
|2 EndNote
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a article
|2 DRIVER
440 _ 0 |0 3091
|a Journal of Biological Chemistry
|v 286
|x 0021-9258
500 _ _ |3 POF3_Assignment on 2016-02-29
500 _ _ |a This work was supported in part by Hungarian National Research Grant 77978.
520 _ _ |a Phosphoglycerate kinase (PGK) is the enzyme responsible for the first ATP-generating step of glycolysis and has been implicated extensively in oncogenesis and its development. Solution small angle x-ray scattering (SAXS) data, in combination with crystal structures of the enzyme in complex with substrate and product analogues, reveal a new conformation for the resting state of the enzyme and demonstrate the role of substrate binding in the preparation of the enzyme for domain closure. Comparison of the x-ray scattering curves of the enzyme in different states with crystal structures has allowed the complete reaction cycle to be resolved both structurally and temporally. The enzyme appears to spend most of its time in a fully open conformation with short periods of closure and catalysis, thereby allowing the rapid diffusion of substrates and products in and out of the binding sites. Analysis of the open apoenzyme structure, defined through deformable elastic network refinement against the SAXS data, suggests that interactions in a mostly buried hydrophobic region may favor the open conformation. This patch is exposed on domain closure, making the open conformation more thermodynamically stable. Ionic interactions act to maintain the closed conformation to allow catalysis. The short time PGK spends in the closed conformation and its strong tendency to rest in an open conformation imply a spring-loaded release mechanism to regulate domain movement, catalysis, and efficient product release.
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|a BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung
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588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Adenosine Triphosphate: chemistry
650 _ 2 |2 MeSH
|a Amino Acid Sequence
650 _ 2 |2 MeSH
|a Animals
650 _ 2 |2 MeSH
|a Binding Sites
650 _ 2 |2 MeSH
|a Biophysics: methods
650 _ 2 |2 MeSH
|a Catalysis
650 _ 2 |2 MeSH
|a Crystallography, X-Ray: methods
650 _ 2 |2 MeSH
|a Humans
650 _ 2 |2 MeSH
|a Mice
650 _ 2 |2 MeSH
|a Molecular Sequence Data
650 _ 2 |2 MeSH
|a Phosphoglycerate Kinase: chemistry
650 _ 2 |2 MeSH
|a Protein Conformation
650 _ 2 |2 MeSH
|a Protein Structure, Secondary
650 _ 2 |2 MeSH
|a Protein Structure, Tertiary
650 _ 2 |2 MeSH
|a Scattering, Radiation
650 _ 2 |2 MeSH
|a Sequence Homology, Amino Acid
650 _ 2 |2 MeSH
|a Thermodynamics
650 _ 7 |0 56-65-5
|2 NLM Chemicals
|a Adenosine Triphosphate
650 _ 7 |0 EC 2.7.2.3
|2 NLM Chemicals
|a Phosphoglycerate Kinase
650 _ 7 |2 WoSType
|a J
700 1 _ |0 P:(DE-Juel1)VDB101252
|a Merli, A.
|b 1
|u FZJ
700 1 _ |0 P:(DE-Juel1)132018
|a Schröder, G.F.
|b 2
|u FZJ
700 1 _ |0 P:(DE-Juel1)VDB101253
|a Varga, A.
|b 3
|u FZJ
700 1 _ |0 P:(DE-Juel1)VDB101254
|a Gráczer, E.
|b 4
|u FZJ
700 1 _ |0 P:(DE-Juel1)VDB101255
|a Pernot, P.
|b 5
|u FZJ
700 1 _ |0 P:(DE-Juel1)VDB101256
|a Round, A.
|b 6
|u FZJ
700 1 _ |0 P:(DE-Juel1)VDB101257
|a Vas, M.
|b 7
|u FZJ
700 1 _ |0 P:(DE-Juel1)VDB101258
|a Bowler, M.W.
|b 8
|u FZJ
773 _ _ |0 PERI:(DE-600)1474604-9
|a 10.1074/jbc.M110.206813
|g Vol. 286, p. 14040 - 14048
|p 14040 - 14048
|q 286<14040 - 14048
|t The @journal of biological chemistry
|v 286
|x 0021-9258
|y 2011
856 7 _ |2 Pubmed Central
|u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3077604
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914 1 _ |y 2011
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