Subunit interactions of transcarboxylase as studied by circular dichroism

Hennessey, John P.; Johnson, W. Curtis; Bahler, Chris R.; Wood, Harland G.

doi:10.1021/bi00533a007

Cited by 25 publications

(7 citation statements)

References 18 publications

(20 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The decrease in helix content corresponded to a dramatic change in the shape of the CD spectra. Such dramatic changes in CD spectra are usually attributed to changes in tertiary (domain organization) or quaternary structure (35,36). These data confirm a FXa structural change (a decrease in a-helix) upon C6PS-induced dimerization and suggest a significant rearrangement of either inter-domain contacts within the protein or secondary structure at the dimer interface.…”

Section: Effect Of Dimerization On Fxa Structuresupporting

confidence: 55%

Functional and Structural Characterization of Factor Xa Dimer in Solution

Chattopadhyay

Iacob

Sen

et al. 2009

Biophysical Journal

View full text Add to dashboard Cite

Previous studies showed that binding of water-soluble phosphatidylserine (C6PS) to bovine factor Xa (FXa) leads to Ca2+-dependent dimerization in solution. We report the effects of Ca2+, C6PS, and dimerization on the activity and structure of human and bovine FXa. Both human and bovine dimers are 10(6)- to 10(7)-fold less active toward prothrombin than the monomer, with the decrease being attributed mainly to a substantial decrease in k(cat). Dimerization appears not to block the active site, since amidolytic activity toward a synthetic substrate is largely unaffected. Circular dichroism reveals a substantial change in tertiary or quaternary structure with a concomitant decrease in alpha-helix upon dimerization. Mass spectrometry identifies a lysine (K(270)) in the catalytic domain that appears to be buried at the dimer interface and is part of a synthetic peptide sequence reported to interfere with factor Va (FVa) binding. C6PS binding exposes K(351) (part of a reported FVa binding region), K(242) (adjacent to the catalytic triad), and K(420) (part of a substrate exosite). We interpret our results to mean that C6PS-induced dimerization produces substantial conformational changes or domain rearrangements such that structural data on PS-activated FXa is required to understand the structure of the FXa dimer or the FXa-FVa complex.

show abstract

Section: Effect Of Dimerization On Fxa Structuresupporting

confidence: 55%

Functional and Structural Characterization of Factor Xa Dimer in Solution

Chattopadhyay

Iacob

Sen

et al. 2009

Biophysical Journal

View full text Add to dashboard Cite

show abstract

“…In Table 2, there were unobvious changes in most components. It was partially consistent with the result described by Hennessey, Johnson, Bahler, and Wood (1982). Nevertheless, the content of 3 10 -helix and anti-aggregated strands increased from 11.32 and 4.89 to about 12.26 and 5.71%, respectively, between the control group and 36 h treatment.…”

Section: Atr-ftirsupporting

confidence: 91%

Influence of malic acid marination on characteristics of connective tissue and textural properties of beefSemitendinosusmuscle

Wang

Tang

2018

CyTA - Journal of Food

View full text Add to dashboard Cite

Semitendinosus muscle marinated in 0.5% acid showed a significant decrease in the shear force. To explore the possible reasons responsible for tenderness of acid-treated beef, the changes in intramuscular connective tissue (IMCT) were taken into consideration. The thicknesses of primary perimysium (PP) and secondary perimysium (SP) decreased to 19.86 and 34.99 μm, respectively. Denaturations of IMCT were exhibited by decreased onset (To) and peak (Tp) temperature, and by the increase in collagen heat solubility. A significant increase in intensity ratios between 3 and 24 h group (p < 0.05) meant that the dissociation of decorin (DCN) enhanced gradually along with marinating time. Meanwhile, limited transitions between 3 10-helix, anti aggregated strands, and turn were observed, especially a significant decrease (p < 0.05) in turn. The dissociation of DCN and the changes in second structures could partially contribute to the initial denaturation of collagen and reduce T O and T P , resulting in the decrease in shear force. Influencia del marinado en ácido málico en las característica del tejido conectivo y las propiedades texturales del músculo semitendinoso de res RESUMEN El presente estudio comprobó que el músculo semitendinoso marinado en 0,5% de ácido presenta una disminución significativa en la fuerza de corte. Para analizar las posibles razones que expliquen la ternura de la carne de res marinada en ácido, se analizaron los cambios detectados en el tejido conectivo intramuscular (IMCT), constatándose que el grosor del perimisio primario (PP) y el perimisio secundario (SP) disminuyó a 19.86 y 34.99 μm, respectivamente. Mediante la aparición disminuida (To), la temperatura máxima (T P) y el aumento de la solubilidad térmica del colágeno, se detectó la desnaturalización del IMCT. Por otra parte, el incremento significativo en las ratios de intensidad en el grupo de entre 3 h y 24 h (p < 0.05) indicó que la disociación de DCN mejoró gradualmente, así también el tiempo de marinado. A su vez, se observaron transiciones limitadas entre la hélice-3 10 , los oligómeros antiagregantes y los giros, constatándose una disminución significativa (p < 0.05) en el giro. Ello lleva a concluir que la disociación de DCN y los cambios en las estructuras secundarias pueden contribuir parcialmente a la desnaturalización inicial del colágeno y reducir T O y T P , provocando la disminución en la fuerza de corte.

show abstract

“…The secondary-structure content was analysed by the principle component regression method using the PLSplus/IQ program of GRAMS/32 (Galactic Industries Corp.). A calibration set of 16 proteins was used as a basis set for the analysis [23].…”

Section: Methodsmentioning

confidence: 99%

Structural analysis of the CD5 antigen

McAlister

Brown

Willis

et al. 1998

European Journal of Biochemistry

View full text Add to dashboard Cite

CD5 is a type-I transmembrane glycoprotein found on thymocytes, T-cells and a subset of B-cells. The extracellular region consists of three domains belonging to the scavenger receptor cysteine-rich (SRCR) superfamily, for which no three-dimensional structure has been obtained. Recombinant soluble CD5 domain 1 (CD5d1), the N-terminal SRCR domain, has been expressed in both chinese hamster ovary (CHO) cells and Pichia pastoris. CD5d1 was shown to be correctly folded by binding to the CD5 monoclonal antibody Leu1. Circular dichroism and NMR analyses indicate that CD5d1 has a high β-sheet content. CD5d1 from both CHO cells and P. pastoris have very similar properties. The disulphide bonding pattern was determined and is consistent with that found for the group-A SRCR domain of type-1 macrophage scavenger receptor and MARCO, the macrophage receptor with collagenous structure. Observations have been made of the role of glycosylation of CD5. P. pastoris expression provides large quantities of correctly folded recombinant CD5d1 for multidimensional NMR and for X-ray crystallographic studies. The whole extracellular region of CD5, expressed as a chimaera with rat CD4 domains 3 and 4 (cCD5d1Ϫ3-CD4d3ϩ4), was studied by electron microscopy and carbohydrate analysis to gain an overview of the structure of the extracellular portion of intact CD5. Carbohydrate analysis identified N-linked glycans on CD5 domains 1 and 2, and sialylated O-linked glycans on the linker peptide between domains 1 and 2. Electron microscopy and carbohydrate analysis together suggest that the extracellular region of CD5 forms a rod-like structure with domain 1 distal from the cell surface and separated from domains 2 and 3 by an O-glycosylated peptide linker region.Keywords : CD5; scavenger receptor cysteine-rich ; glycosylation; disulphide bonds ; NMR spectroscopy.The cell surface glycoprotein CD5 is expressed on thymocytes, T lymphocytes and some B cells [1]. Functional data including studies of knock-out mice point to a role for CD5 in the control of lymphocyte responses (e.g. [2,3] 118 , CD5d1 residues 1Ϫ118 expressed in CHO cells ; cCD5d1Ϫ3-CD4d3ϩ4, a chimaera consisting of the entire extracellular region of human or rat CD5 fused to domains 3 and 4 of rat CD4; cCD5d1-CD4d3ϩ4, a chimaera of human CD5 residues 1Ϫ118 fused to rat CD4 domains 3 and 4; pCD5110, CD5d1 residues 1Ϫ110 expressed in Pichia pastoris ; CHO, chinese hamster ovary cells ; endo, endoglycosidase; ESI-MS, electrospray ionisation mass spectroscopy; gu, glucose units; MALDI-MS, matrix-assisted laser-desorption ionisation mass spectroscopy ; SEC, size-exclusion chromatography; SRCR, scavenger receptor cysteine-rich superfamily; WAX, weak anion-exchange chromatography. three scavenger receptor cysteine-rich (SRCR) domains [4]. In structure and tissue distribution CD5 resembles CD6 which has three SRCR domains [5,6] and SPA which also has three SRCR domains but is a soluble protein that binds to macrophages [7]. SRCR domains are found in various cell surface antigens of leukocytes ...

show abstract

Subunit interactions of transcarboxylase as studied by circular dichroism

Cited by 25 publications

References 18 publications

Functional and Structural Characterization of Factor Xa Dimer in Solution

Functional and Structural Characterization of Factor Xa Dimer in Solution

Influence of malic acid marination on characteristics of connective tissue and textural properties of beefSemitendinosusmuscle

Structural analysis of the CD5 antigen

Contact Info

Product

Resources

About