Narrowing the conformational space sampled by two-domain proteins with paramagnetic probes in both domains

被引：38

作者：

Dasgupta, Soumyasri ^{[1
]}

Hu, Xiaoyu ^{[1
]}

Keizers, Peter H. J. ^{[2
]}

Liu, Wei-Min ^{[2
]}

Luchinat, Claudio ^{[1
,3
]}

Nagulapalli, Malini ^{[1
]}

Overhand, Mark ^{[2
]}

Parigi, Giacomo ^{[1
,3
]}

Sgheri, Luca ^{[4
]}

Ubbink, Marcellus ^{[2
]}

机构：

[1] Univ Florence, Magnet Resonance Ctr CERM, I-50019 Sesto Fiorentino, Italy

[2] Leiden Univ, Leiden Inst Chem, Gorlaeus Labs, NL-2300 RA Leiden, Netherlands

[3] Univ Florence, Dept Chem, I-50019 Sesto Fiorentino, Italy

[4] CNR, Ist Applicaz Calcolo, Sez Firenze, I-50019 Sesto Fiorentino, Italy

来源：

JOURNAL OF BIOMOLECULAR NMR | 2011年 / 51卷 / 03期

关键词：

Conformational heterogeneity; Maximum allowed probability; Maximum occurrence; Paramagnetic proteins; Paramagnetic tag; Calmodulin; RESIDUAL DIPOLAR COUPLINGS; ELECTRON-TRANSFER COMPLEX; CYTOCHROME-C PEROXIDASE; NMR-SPECTROSCOPY; PSEUDOCONTACT SHIFTS; RELAXATION DISPERSION; CALMODULIN; BINDING; DYNAMICS; METALLOPROTEINS;

D O I：

10.1007/s10858-011-9532-2

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Calmodulin is a two-domain protein which in solution can adopt a variety of conformations upon reorientation of its domains. The maximum occurrence (MO) of a set of calmodulin conformations that are representative of the overall conformational space possibly sampled by the protein, has been calculated from the paramagnetism-based restraints. These restraints were measured after inclusion of a lanthanide binding tag in the C-terminal domain to supplement the data obtained by substitution of three paramagnetic lanthanide ions to the calcium ion in the second calcium binding loop of the N-terminal domain. The analysis shows that the availability of paramagnetic restraints arising from metal ions placed on both domains, reduces the MO of the conformations to different extents, thereby helping to identify those conformations that can be mostly sampled by the protein.

引用

页码：253 / 263

页数：11

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