1IBI

QUAIL CYSTEINE AND GLYCINE-RICH PROTEIN, NMR, 15 MINIMIZED MODEL STRUCTURES

Summary for 1IBI

• Entry DOI: 10.2210/pdb1ibi/pdb
• Related: 1QLI
• NMR Information: BMRB: 5065
• Descriptor: CYSTEINE-RICH PROTEIN 2, ZINC ION (2 entities in total)
• Functional Keywords: lim domain containing proteins, metal-binding protein, metal binding protein
• Biological source: Coturnix japonica (Japanese quail)
• Total number of polymer chains: 1
• Total formula weight: 12256.59

Authors

Schuler, W.,Kloiber, K.,Matt, T.,Bister, K.,Konrat, R. (deposition date: 2001-03-28, release date: 2001-09-05, Last modification date: 2024-05-22)

Primary citation

Schuler, W.,Kloiber, K.,Matt, T.,Bister, K.,Konrat, R.
Application of cross-correlated NMR spin relaxation to the zinc-finger protein CRP2(LIM2): evidence for collective motions in LIM domains.
Biochemistry, 40:9596-9604, 2001

PubMed Abstract: The solution structure of quail CRP2(LIM2) was significantly improved by using an increased number of NOE constraints obtained from a 13C,15N-labeled protein sample and by applying a recently developed triple-resonance cross-correlated relaxation experiment for the determination of the backbone dihedral angle psi. Additionally, the relative orientation of the 15N(i)-1HN(i) dipole and the 13CO(i) CSA tensor, which is related to both backbone angles phi and psi, was probed by nitrogen-carbonyl multiple-quantum relaxation and used as an additional constraint for the refinement of the local geometry of the metal-coordination sites in CRP2(LIM2). The backbone dynamics of residues located in the folded part of CRP2(LIM2) have been characterized by proton-detected 13C'(i-1)-15N(i) and 15N(i)-1HN(i) multiple-quantum relaxation, respectively. We show that regions having cross-correlated time modulation of backbone isotropic chemical shifts on the millisecond to microsecond time scale correlate with residues that are structurally altered in the mutant protein CRP2(LIM2)R122A (disruption of the CCHC zinc-finger stabilizing side-chain hydrogen bond) and that these residues are part of an extended hydrogen-bonding network connecting the two zinc-binding sites. This indicates the presence of long-range collective motions in the two zinc-binding subdomains. The conformational plasticity of the LIM domain may be of functional relevance for this important protein recognition motif.

PubMed: 11583159
DOI: 10.1021/bi010509m

Experimental method

SOLUTION NMR