1nps

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CRYSTAL STRUCTURE OF N-TERMINAL DOMAIN OF PROTEIN S

File:1nps.gif


1nps, resolution 1.8Å

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OverviewOverview

Protein S from Myxococcus xanthus is a member of the beta gamma-crystallin, superfamily. Its N and C-terminal domains (NPS and CPS, respectively) show, a high degree of structural similarity and possess the capacity to bind, two calcium ions per domain. For NPS, their positions were determined by, X-ray diffraction at 1.8 A resolution, making use of molecular replacement, with the NMR structure as search model. The overall topology of NPS is, found to be practically the same as in complete protein S. In natural, protein S, the domains fold independently, with a significant increase in, stability and cooperativity of folding in the presence of Ca2+. The, recombinant isolated domains are stable monomers which do not show any, tendency to combine to "nicked" full-length protein S. In order to, investigate the stability and folding of natural protein S and its, isolated domains, spectroscopic techniques were applied, measuring the, reversible urea and temperature-induced unfolding transitions at varying, pH. The increment of Ca2+ to the free energy of stabilization amounts to, -10 and -5 kJ/mol for NPS and CPS, respectively. For both NPS and CPS, in, the absence and in the presence of 3 mM CaCl2, the two-state model is, valid. Comparing DeltaGU-->N for CPS (-21 kJ/mol at pH 7, liganded with, Ca2+) with its increment in the intact two-domain protein, the stability, of the isolated domain turns out to be decreased in a pH-dependent manner., In contrast, the stability of Ca2+-loaded NPS (DeltaGU-->N=-31 kJ/mol, pH, 7) is nearly unchanged down to pH 2 where Ca2+ is released, (DeltaGU-->N=-26 kJ/mol, pH 2). In intact protein S, the N-terminal domain, is destabilized relative to NPS. Evidently, apart from Ca2+ binding, well-defined domain interactions contribute significantly to the overall, stability of intact protein S.

About this StructureAbout this Structure

1NPS is a Single protein structure of sequence from Myxococcus xanthus with CA as ligand. Full crystallographic information is available from OCA.

ReferenceReference

The domains of protein S from Myxococcus xanthus: structure, stability and interactions., Wenk M, Baumgartner R, Holak TA, Huber R, Jaenicke R, Mayr EM, J Mol Biol. 1999 Mar 12;286(5):1533-45. PMID:10064714

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