Importance of Thr-353 of the conserved phosphorylation loop of the sarcoplasmic reticulum Ca2+-ATPase in MgATP binding and catalytic activity. - Wikidata - awgldk - TriplyDB

Importance of Thr-353 of the conserved phosphorylation loop of the sarcoplasmic reticulum Ca2+-ATPase in MgATP binding and catalytic activity.

Importance of Thr-353 of the conserved phosphorylation loop of the sarcoplasmic reticulum Ca2+-ATPase in MgATP binding and catalytic activity.

http://www.wikidata.org/entity/Q43662774

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SERCA mutant E309Q binds two Ca2+ions but adopts a catalytically incompetent conformation Importance of conserved Thr214 in domain A of the Na+,K+ -ATPase for stabilization of the phosphoryl transition state complex in E2P dephosphorylation Roles of conserved P domain residues and Mg2+ in ATP binding in the ground and Ca2+-activated states of sarcoplasmic reticulum Ca2+-ATPase.Mutational analysis of the conserved TGES loop of sarcoplasmic reticulum Ca2+-ATPase.Probing Mechanistic Similarities between Response Regulator Signaling Proteins and Haloacid Dehalogenase Phosphatases.Focus on phosphoaspartate and phosphoglutamate.Diversification of function in the haloacid dehalogenase enzyme superfamily: The role of the cap domain in hydrolytic phosphoruscarbon bond cleavage.Thapsigargin and dimethyl sulfoxide activate medium P(i)<-->HOH oxygen exchange catalyzed by sarcoplasmic reticulum Ca2+-ATPase.Mapping interactions between the Ca2+-ATPase and its substrate ATP with infrared spectroscopy.Importance of conserved N-domain residues Thr441, Glu442, Lys515, Arg560, and Leu562 of sarcoplasmic reticulum Ca2+-ATPase for MgATP binding and subsequent catalytic steps. Plasticity of the nucleotide-binding site.Expression of Na+,K+-ATPase in Pichia pastoris: analysis of wild type and D369N mutant proteins by Fe2+-catalyzed oxidative cleavage and molecular modeling.Functional cloning of the miltefosine transporter. A novel P-type phospholipid translocase from Leishmania involved in drug resistance.Critical interaction of actuator domain residues arginine 174, isoleucine 188, and lysine 205 with modulatory nucleotide in sarcoplasmic reticulum Ca2+-ATPase.Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues.Functional consequences of alterations to Thr247, Pro248, Glu340, Asp813, Arg819, and Arg822 at the interfaces between domain P, M3, and L6-7 of sarcoplasmic reticulum Ca2+-ATPase. Roles in Ca2+ interaction and phosphoenzyme processing.Evidence calcium pump binds magnesium before inorganic phosphate.Asparagine 706 and glutamate 183 at the catalytic site of sarcoplasmic reticulum Ca2+-ATPase play critical but distinct roles in E2 states.Mutations Phe785Leu and Thr618Met in Na+,K+-ATPase, associated with familial rapid-onset dystonia parkinsonism, interfere with Na+ interaction by distinct mechanisms.ATP-binding modes and functionally important interdomain bonds of sarcoplasmic reticulum Ca2+-ATPase revealed by mutation of glycine 438, glutamate 439, and arginine 678.

P2860

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P2860

Importance of Thr-353 of the conserved phosphorylation loop of the sarcoplasmic reticulum Ca2+-ATPase in MgATP binding and catalytic activity.

http://www.wikidata.org/entity/Q43662774

description

2001 nî lūn-bûn

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2001年の論文

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2001年学术文章

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2001年学术文章

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2001年学术文章

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2001年学术文章

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2001年学术文章

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2001年学术文章

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2001年學術文章

@yue

2001年學術文章

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name

Importance of Thr-353 of the c ...... inding and catalytic activity.

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Importance of Thr-353 of the c ...... inding and catalytic activity.

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type

label

Importance of Thr-353 of the c ...... inding and catalytic activity.

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Importance of Thr-353 of the c ...... inding and catalytic activity.

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prefLabel

Importance of Thr-353 of the c ...... inding and catalytic activity.

@en

Importance of Thr-353 of the c ...... inding and catalytic activity.

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Journal of Biological Chemistry

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Importance of Thr-353 of the c ...... inding and catalytic activity.

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Andersen JP

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Clausen JD

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McIntosh DB

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Woolley DG

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P2860

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution

The crystal structure of bacillus cereus phosphonoacetaldehyde hydrolase: insight into catalysis of phosphorus bond cleavage and catalytic diversification within the HAD enzyme superfamily

Crystal structure of an activated response regulator bound to its target

Crystal structure of phosphoserine phosphatase from Methanococcus jannaschii, a hyperthermophile, at 1.8 A resolution

Magnesium binding to the bacterial chemotaxis protein CheY results in large conformational changes involving its functional surface

Crystal structure of L-2-haloacid dehalogenase from Pseudomonas sp. YL. An alpha/beta hydrolase structure that is different from the alpha/beta hydrolase fold

High-efficiency transformation of mammalian cells by plasmid DNA

Mechanistic studies of phosphoserine phosphatase, an enzyme related to P-type ATPases

A new class of phosphotransferases phosphorylated on an aspartate residue in an amino-terminal DXDX(T/V) motif

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35741-35750

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10.1074/JBC.M105434200

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38

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276

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11438551

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phosphorylation