PDBsum entry 1u06

Structural protein

PDB id: 1u06

Contents

Protein chain

55 a.a. *

Ligands

AZI ×3

Waters ×53

* Residue conservation analysis

PDB id:

1u06

Name:

Structural protein

Title:

Crystal structure of chicken alpha-spectrin sh3 domain

Structure:

Spectrin alpha chain, brain. Chain: a. Fragment: sh3 domain. Synonym: spectrin, non-erythroid alpha chain, fodrin alpha chain. Engineered: yes

Source:

Gallus gallus. Chicken. Organism_taxid: 9031. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

1.49Å R-factor: 0.176 R-free: 0.189

Authors:

V.Chevelkov,K.Faelber,A.Diehl,U.Heinemann,H.Oschkinat,B.Reif

Key ref:

V.Chevelkov et al. (2005). Detection of dynamic water molecules in a microcrystalline sample of the SH3 domain of alpha-spectrin by MAS solid-state NMR. J Biomol Nmr, 31, 295-310. PubMed id: 15928996

Date:

13-Jul-04 Release date: 13-Jan-05

Protein chain

P07751  (SPTN1_CHICK) -  Spectrin alpha chain, non-erythrocytic 1 from Gallus gallus

Seq: 2477 a.a.

Struc: 55 a.a.

J Biomol Nmr 31:295-310 (2005)

PubMed id: 15928996

Detection of dynamic water molecules in a microcrystalline sample of the SH3 domain of alpha-spectrin by MAS solid-state NMR.

V.Chevelkov, K.Faelber, A.Diehl, U.Heinemann, H.Oschkinat, B.Reif.

ABSTRACT

Water molecules are a major determinant of protein stability and are important for understanding protein-protein interactions. We present two experiments which allow to measure first the effective T(2) decay rate of individual amide proton, and second the magnetization build-up rates for a selective transfer from H(2)O to H(N) using spin diffusion as a mixing element. The experiments are demonstrated for a uniformly (2)H, (15)N labeled sample of a microcrystalline SH3 domain in which exchangeable deuterons were back-substituted with protons. In order to evaluate the NMR experimental data, as X-ray structure of the protein was determined using the same crystallization protocol as for the solid-state NMR sample. The NMR experimental data are correlated with the dipolar couplings calculated from H(2)O-H(N) distances which were extracted from the X-ray structure of the protein. We find that the H(N) T(2) decay rates and H(2)O-H(N) build-up rates are sensitive to distance and dynamics of the detected water molecules with respect to the protein. We show that qualitative information about localization and dynamics of internal water molecules can be obtained in the solid-state by interpretation of the spin dynamics of a reporter amide proton.