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PDBsum entry 1ibi

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protein metals links
Metal binding protein PDB id
1ibi

 

 

 

 

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Contents
Protein chain
59 a.a. *
Metals
_ZN ×2
* Residue conservation analysis
PDB id:
1ibi
Name: Metal binding protein
Title: Quail cysteine and glycine-rich protein, nmr, 15 minimized model structures
Structure: Cysteine-rich protein 2. Chain: a. Fragment: c-terminal lim domain, residues 82-194. Synonym: crp2. Engineered: yes
Source: Coturnix japonica. Japanese quail. Organism_taxid: 93934. Gene: csrp2. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 15 models
Authors: W.Schuler,K.Kloiber,T.Matt,K.Bister,R.Konrat
Key ref:
W.Schüler et al. (2001). 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. PubMed id: 11583159 DOI: 10.1021/bi010509m
Date:
28-Mar-01     Release date:   05-Sep-01    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q05158  (CSRP2_COTJA) -  Cysteine and glycine-rich protein 2 from Coturnix japonica
Seq:
Struc:
194 a.a.
59 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
DOI no: 10.1021/bi010509m Biochemistry 40:9596-9604 (2001)
PubMed id: 11583159  
 
 
Application of cross-correlated NMR spin relaxation to the zinc-finger protein CRP2(LIM2): evidence for collective motions in LIM domains.
W.Schüler, K.Kloiber, T.Matt, K.Bister, R.Konrat.
 
  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.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
16786593 K.Loth, D.Abergel, P.Pelupessy, M.Delarue, P.Lopes, J.Ouazzani, N.Duclert-Savatier, M.Nilges, G.Bodenhausen, and V.Stoven (2006).
Determination of dihedral Psi angles in large proteins by combining NH(N)/C(alpha)H(alpha) dipole/dipole cross-correlation and chemical shifts.
  Proteins, 64, 931-939.  
12794636 A.Velyvis, J.Vaynberg, Y.Yang, O.Vinogradova, Y.Zhang, C.Wu, and J.Qin (2003).
Structural and functional insights into PINCH LIM4 domain-mediated integrin signaling.
  Nat Struct Biol, 10, 558-564.
PDB code: 1nyp
12727888 J.E.Deane, J.P.Mackay, A.H.Kwan, E.Y.Sum, J.E.Visvader, and J.M.Matthews (2003).
Structural basis for the recognition of ldb1 by the N-terminal LIM domains of LMO2 and LMO4.
  EMBO J, 22, 2224-2233.
PDB codes: 1j2o 1m3v
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.

 

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