Solution Structure and Calcium-Binding Properties of M-Crystallin, A Primordial βγ-Crystallin from Archaea

Barnwal, Ravi Pratap; Jobby, Maroor K.; Devi, Kavita; Sharma, Yogendra; Chary, Kandala V. R.

doi:10.1016/j.jmb.2008.12.058

Cited by 54 publications

(79 citation statements)

References 63 publications

(86 reference statements)

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“…1d). This arrangement is common in the ␤␥ domains studied structurally: Protein S (33), Spherulin 3a (22), Ci-␤␥-crystallin (40), Clostrillin, Flavollin, M-crystallin (23,41), and Geodin (42).…”

Section: Architecture Of the ␤␥-Crystallin-type Ca 2؉ -Binding Motifmentioning

confidence: 89%

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Ca2+-binding Motif of βγ-Crystallins

Srivastava¹,

Mishra

Krishnan³

et al. 2014

Journal of Biological Chemistry

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␤␥-Crystallin-type double clamp (N/D)(N/D)XX(S/T)S motif is an established but sparsely investigated motif for Ca2؉ binding. A ␤␥-crystallin domain is formed of two Greek key motifs, accommodating two Ca 2؉ -binding sites. ␤␥-Crystallins make a separate class of Ca 2؉ -binding proteins (CaBP), apparently a major group of CaBP in bacteria. Paralleling the diversity in ␤␥-crystallin domains, these motifs also show great diversity, both in structure and in function. Although the expression of some of them has been associated with stress, virulence, and adhesion, the functional implications of Ca 2؉ binding to ␤␥-crystallins in mediating biological processes are yet to be elucidated.

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Section: Architecture Of the ␤␥-Crystallin-type Ca 2؉ -Binding Motifmentioning

confidence: 89%

“…It is clear that the ␤␥-crystallin domain is widely spread. However, it has been difficult to assign functions in many ␤␥-crystallins studied so far (22,23,38,41,40,83,87,88). Protein S of M. xanthus is expressed as a soluble protein and selfassembles as a multilayer spore coat in a Ca 2ϩ -dependent manner.…”

Section: ؉ Binding and Domain Stabilizationmentioning

confidence: 99%

Ca2+-binding Motif of βγ-Crystallins

Srivastava¹,

Mishra

Krishnan³

et al. 2014

Journal of Biological Chemistry

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“…They have a major role in generating the lens's high transparency and high refractive index (Mahendiran et al 2014;. This protein family is believed to have originated from primordial Archaeabacteria as single-domain Ca 2+ binding proteins (Barnwal et al 2009;Mishra et al 2014). The βγ-crystallins are ubiquitous in the eyes of mammals, and in Fig.…”

Section: βγ-Crystallinsmentioning

confidence: 99%

Biophysical chemistry of the ageing eye lens

Ray

2015

Biophys Rev

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This review examines both recent and historical literature related to the biophysical chemistry of the proteins in the ageing eye, with a particular focus on cataract development. The lens is a vital component of the eye, acting as an optical focusing device to form clear images on the retina. The lens maintains the necessary high transparency and refractive index by expressing crystallin proteins in high concentration and eliminating all large cellular structures that may cause light scattering. This has the consequence of eliminating lens fibre cell metabolism and results in mature lens fibre cells having no mechanism for protein expression and a complete absence of protein recycling or turnover. As a result, the crystallins are some of the oldest proteins in the human body. Lack of protein repair or recycling means the lens tends to accumulate damage with age in the form of protein posttranslational modifications. The crystallins can be subject to a wide range of age-related changes, including isomerisation, deamidation and racemisation. Many of these modification are highly correlated with cataract formation and represent a biochemical mechanism for age-related blindness.

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“…Although the ancestral function of the βγ -crystallin superfamily remains unclear, the existence of the urochordate Ci-βγ crystallin 7 suggests that the emergence of this protein fold predates the evolution of eye lenses and may be related to calcium-binding proteins. 8,9 The α-crystallins are small heat-shock proteins (HSPs) that are closely related to each other and to other chaperone proteins in a great variety of organisms. 10,11 They bind to and solubilize misfolded or otherwise aggregation-prone structural proteins but lack the ability to refold them, 12 because, in nonlens contexts, they work in concert with ATP-dependent refolding chaperones.…”

Section: Introductionmentioning

confidence: 99%

NMR Studies of Eye Lens Crystallins

Martin

2014

eMagRes

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The crystallins of the eye lens are highly stable, soluble proteins that generate the refractive index gradient of the lens. In their native context, the crystallins form large soluble oligomers; a loss in solubility due to mutation, UV light damage, or chemical modification results in cataract. There are two broad classes of ubiquitous crystallin proteins; βγ -crystallins, which are purely structural, and the α-crystallins, which additionally play a chaperone role, maintaining solubility of compromised proteins in the lens. NMR methods have been used to investigate many structural and functional properties of both types of crystallins. Structures have been solved for many of the crystallins using both solid-state and solution NMRs, and these detailed molecular pictures have been used as a starting point for investigating conformational dynamics and intermolecular interactions.

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Solution Structure and Calcium-Binding Properties of M-Crystallin, A Primordial βγ-Crystallin from Archaea

Cited by 54 publications

References 63 publications

Ca2+-binding Motif of βγ-Crystallins

Ca2+-binding Motif of βγ-Crystallins

Biophysical chemistry of the ageing eye lens

NMR Studies of Eye Lens Crystallins

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