scholarly journals Crystal structure of ADP-dependent glucokinase from Methanocaldococcus jannaschii in complex with 5-iodotubercidin reveals phosphoryl transfer mechanism

2018 ◽  
Vol 27 (3) ◽  
pp. 790-797 ◽  
Author(s):  
Piotr Tokarz ◽  
Magdalena Wiśniewska ◽  
Marcin M. Kamiński ◽  
Grzegorz Dubin ◽  
Przemysław Grudnik
Keyword(s):  
Crystal Structure ◽  
Transfer Mechanism ◽  
Phosphoryl Transfer ◽  
Methanocaldococcus Jannaschii

Crystal structure of NusG N-terminal (NGN) domain from Methanocaldococcus jannaschii and its interaction with rpoE″

2009 ◽  
Vol 76 (4) ◽  
pp. 787-793 ◽  
Author(s):  
Huihao Zhou ◽  
Qi Liu ◽  
Yongxiang Gao ◽  
Maikun Teng ◽  
Liwen Niu
Keyword(s):  
Crystal Structure ◽  
Methanocaldococcus Jannaschii

Crystal structure analysis of a hypothetical protein (MJ0366) from Methanocaldococcus jannaschii revealed a novel topological arrangement of the knot fold

2017 ◽  
Vol 482 (2) ◽  
pp. 264-269 ◽  
Author(s):  
Viswanathan Thiruselvam ◽  
Thirumananseri Kumarevel ◽  
Ponnuraj Karthe ◽  
Seiki Kuramitsu ◽  
Shigeyuki Yokoyama ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Structure Analysis ◽  
Hypothetical Protein ◽  
Crystal Structure Analysis ◽  
Methanocaldococcus Jannaschii

scholarly journals The crystal structure ofMycobacterium tuberculosisadenylate kinase in complex with two molecules of ADP and Mg2+supports an associative mechanism for phosphoryl transfer

2006 ◽  
Vol 15 (6) ◽  
pp. 1489-1493 ◽  
Author(s):  
Marco Bellinzoni ◽  
Ahmed Haouz ◽  
Martin Graña ◽  
Hélène Munier-Lehmann ◽  
William Shepard ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Phosphoryl Transfer ◽  
Associative Mechanism

scholarly journals How a Second Mg2+ Ion Affects the Phosphoryl-Transfer Mechanism in a Protein Kinase: A Computational Study

ACS Catalysis ◽  
2020 ◽  
Vol 11 (1) ◽  
pp. 169-183
Author(s):  
Rodrigo Recabarren ◽  
Kirill Zinovjev ◽  
Iñaki Tuñón ◽  
Jans Alzate-Morales
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Computational Study ◽  
Transfer Mechanism ◽  
Phosphoryl Transfer ◽  
Kinase A

scholarly journals Study of the Phosphoryl-Transfer Mechanism of Shikimate Kinase by NMR Spectroscopy

2016 ◽  
Vol 22 (8) ◽  
pp. 2758-2768 ◽  
Author(s):  
Verónica Prado ◽  
Emilio Lence ◽  
Juan A. Vallejo ◽  
Alejandro Beceiro ◽  
Paul Thompson ◽  
...  
Keyword(s):  
Nmr Spectroscopy ◽  
Transfer Mechanism ◽  
Phosphoryl Transfer ◽  
Shikimate Kinase

scholarly journals Structures of substrate- and nucleotide-bound propionate kinase fromSalmonella typhimurium: substrate specificity and phosphate-transfer mechanism

2015 ◽  
Vol 71 (8) ◽  
pp. 1640-1648 ◽  
Author(s):  
Ambika Mosale Venkatesh Murthy ◽  
Subashini Mathivanan ◽  
Sagar Chittori ◽  
Handanahal Subbarao Savithri ◽  
Mathur Ramabhadrashastry Narasimha Murthy
Keyword(s):  
Substrate Specificity ◽  
Crystal Structures ◽  
Active Site ◽  
Structural Data ◽  
Transfer Mechanism ◽  
Phosphoryl Group ◽  
Phosphoryl Transfer ◽  
Active Site Pocket ◽  
Bipyramidal Structure

Kinases are ubiquitous enzymes that are pivotal to many biochemical processes. There are contrasting views on the phosphoryl-transfer mechanism in propionate kinase, an enzyme that reversibly transfers a phosphoryl group from propionyl phosphate to ADP in the final step of non-oxidative catabolism of L-threonine to propionate. Here, X-ray crystal structures of propionate- and nucleotide-boundSalmonella typhimuriumpropionate kinase are reported at 1.8–2.0 Å resolution. Although the mode of nucleotide binding is comparable to those of other members of the ASKHA superfamily, propionate is bound at a distinct site deeper in the hydrophobic pocket defining the active site. The propionate carboxyl is at a distance of ∼5 Å from the γ-phosphate of the nucleotide, supporting a direct in-line transfer mechanism. The phosphoryl-transfer reaction is likely to occurviaan associative SN2-like transition state that involves a pentagonal bipyramidal structure with the axial positions occupied by the nucleophile of the substrate and the O atom between the β- and the γ-phosphates, respectively. The proximity of the strictly conserved His175 and Arg236 to the carboxyl group of the propionate and the γ-phosphate of ATP suggests their involvement in catalysis. Moreover, ligand binding does not induce global domain movement as reported in some other members of the ASKHA superfamily. Instead, residues Arg86, Asp143 and Pro116-Leu117-His118 that define the active-site pocket move towards the substrate and expel water molecules from the active site. The role of Ala88, previously proposed to be the residue determining substrate specificity, was examined by determining the crystal structures of the propionate-bound Ala88 mutants A88V and A88G. Kinetic analysis and structural data are consistent with a significant role of Ala88 in substrate-specificity determination. The active-site pocket-defining residues Arg86, Asp143 and the Pro116-Leu117-His118 segment are also likely to contribute to substrate specificity.

Crystal structure, energy transfer mechanism and tunable luminescence in Ce3+/Dy3+ co-activated Ca20Mg3Al26Si3O68 nanophosphors

2016 ◽  
Vol 42 (9) ◽  
pp. 10854-10865 ◽  
Author(s):  
Ashwini Kumar ◽  
S.J. Dhoble ◽  
D.R. Peshwe ◽  
Jatin Bhatt ◽  
J.J. Terblans ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Energy Transfer ◽  
Transfer Mechanism ◽  
Energy Transfer Mechanism
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