Conformations of carp muscle calcium binding parvalbumin

Donato, Henry; Rb, Martin

doi:10.1021/bi00719a016

Cited by 98 publications

(55 citation statements)

References 15 publications

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“…Of the two Ca (II) of parvalbumin, Ca (EF) is overlaid within 0.5 nm by the aromatic side chain of Phe-57. Upon substitution of Ca (II) by terbium (III) and irradiation at 259 nm a characteristic green Tb (III) emission appears, due-to energy transfer from the aromatic side chain of Phe-57 to Tb (EF) [6,9]. Tb (III) emission also occurs upon substitution of the lanthanide ion for Ca (II) in TN-C.…”

Section: Introductionmentioning

confidence: 99%

Calcium binding sites of rabbit troponin and carp parvalbumin

et al. 1975

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Section: Introductionmentioning

confidence: 99%

Calcium binding sites of rabbit troponin and carp parvalbumin

et al. 1975

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“…The substitution of the two Ca2+ by Tb3+ was performed using a procedure similar to that described in [15]. The extent of replacement was first followed by fluorescence measurement and titration of a parvalbumin solution (0.08 FM) in 30 mM imidazoie, 10 mM NaN3 (pH 6.6) by a solution 6.4 mM TbCl3 in water.…”

Section: Methodsmentioning

confidence: 99%

“…The determination of this structure at high resolution is interesting for 3 reasons. Firstly, information has been collected using Tb3+ and other lanthanides as luminescence probes in carp [15,16] and cod parvalbumin [17-191 through radiationless energy transfer between aromatic amino acids, excited in their UV absorption bands and the lanthanide which, in this way, is sensitized to emit strongly. Secondly, new methods are developing in macromolecular crystallography.…”

Section: Introductionmentioning

confidence: 99%

Crystallization and structure at 3.2 Å resolution of a terbium parvalbumin

et al. 1985

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Toadfish muscle parvalbumin I& can bind two Tb3+ which displace the two Caz+ normally bound. This terbium derivative was crystallized with space group P2,2,2 and lattice constants a= 56.2 A, b = 59.5 A and c = 27.2 A. The structure at 3.2 A resolution was determined applying a molecular replacement method and using the known co-ordinates of carp Caz+-parvalbumin. The structure was refined to a conventional R factor of 26 % for 1166 reflections in the resolution range 3.2-6 A. The a-carbon backbone of the structures of toadtish and carp parvalbumins are very similar.Crystal X-ray crystallography Three-dimensional structure TF+ Parvalbumin Ca2+-binding site

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“…Both troponin C and parvalbumin are able to interact with calcium even in the presence of high concentrations of urea (17,35), suggesting that the calcium-protein complex is highly stable and can resist the denaturing effect of strong urea solutions. Troponin C binds calcium in 6 M urea with a small increase in electrophoretic mobility; if, however, the Mg-ATPase inhibitory protein (troponin I) is also present in the calcium-urea gel, the two proteins interact, forming a slower migrating complex (17).…”

Section: A Comparison With Other Contractile and Calcium-binding Systemsmentioning

confidence: 99%

“…Thus, both the calciumbinding site(s) and the troponin I recognition site of the troponin C molecule retain their integrity in 6 M urea. Similarly, parvalbumin undergoes a conformational change on addition of calcium in solutions containing 4 M urea (35).…”

Section: A Comparison With Other Contractile and Calcium-binding Systemsmentioning

confidence: 99%

Calcium-binding proteins in the vorticellid spasmoneme

Lm¹

1978

The Journal of Cell Biology

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The proteins of the contractile spasmoneme from Vorticella convallaria, Carchesium polypinum, and Zoothamnium geniculatum have been extracted in the detergent, sodium dodecyl sulfate (SDS), as well as urea and guanidine hydrochloride (GuCl). After SDS extraction, the molecular weight distribution of the proteins was examined by means of SDS-polyacrylamide gel electrophoresis. Significant amounts of material corresponding to the contractile proteins actin and tubulin are not present.The contractile organelles in the three species examined contain a group of closely related proteins of molecular weight near 20,000, which constitute a major part (40-60%) of the dry mass. The 20,000 mol wt proteins in Zoothamnium bind calcium with high affinity (pK -~ 6) and are termed "spasmins." By means of urea polyacrylamide gel electrophoresis, it is demonstrated that in Carchesium and Zoothamnium certain spasmin components bind calcium even in the presence of 6 M urea. The binding of calcium in 6 M urea suggests a functional relationship between the spasmins and the calcium-binding proteins of striated muscle which behave similarly. The calcium binding in urea also indicates that the spasmins within a single spasmoneme have different calcium affinities, and this difference in calcium-binding properties may be an important factor in the physiological function of the organelle. KEY WORDS contraction calcium Vorticella spasmonemeSeveral species of ciliated protozoa exhibit a rapid form of contraction. This is particularly clear in the stalked peritrichous ciliates, Vorticella, Carchesium, and Zoothamnium, which, on contraction, throw their stalks into tight helical coils or folds. Within the stalk is the contractile organelle, often referred to as the myoneme (1), though the term spasmoneme (2) is preferable since recent studies indicate that the organelle is biochemically distinct from the myosin-and actin-based contractile systems (3).The spasmoneme contracts within 2-10 ms (4, 5), and the shortening velocity may be as high as 172 lengths/s, whereas the extension phase is of the order of seconds. The contraction velocity of the spasmoneme in Zoothamnium, (measured in lengths/second), is thus nine times greater than in 358J. CELL BIOLOGY 9 The Rockefeller University Press 9

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Conformations of carp muscle calcium binding parvalbumin

Cited by 98 publications

References 15 publications

Calcium binding sites of rabbit troponin and carp parvalbumin

Calcium binding sites of rabbit troponin and carp parvalbumin

Crystallization and structure at 3.2 Å resolution of a terbium parvalbumin

Calcium-binding proteins in the vorticellid spasmoneme

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