spacer
spacer

PDBsum entry 2gle

Go to PDB code: 
protein links
Protein binding PDB id
2gle
Jmol
Contents
Protein chain
74 a.a. *
* Residue conservation analysis
PDB id:
2gle
Name: Protein binding
Title: Solution structure of neurabin sam domain
Structure: Neurabin-1. Chain: a. Fragment: sam domain (residues 986-1056). Synonym: neurabin-i, neural tissue-specific f-actin- binding protein i, protein phosphatase 1 regulatory subunit 9a, p180, pp1bp175. Engineered: yes
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Expressed in: escherichia coli. Expression_system_taxid: 562. Pet28a
NMR struc: 20 models
Authors: T.Ju,J.Hudak,W.Peti
Key ref:
T.Ju et al. (2007). Structural characterization of the neurabin sterile alpha motif domain. Proteins, 69, 192-198. PubMed id: 17600833 DOI: 10.1002/prot.21513
Date:
04-Apr-06     Release date:   13-Mar-07    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
O35867  (NEB1_RAT) -  Neurabin-1
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1095 a.a.
74 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 

 
DOI no: 10.1002/prot.21513 Proteins 69:192-198 (2007)
PubMed id: 17600833  
 
 
Structural characterization of the neurabin sterile alpha motif domain.
T.Ju, M.J.Ragusa, J.Hudak, A.C.Nairn, W.Peti.
 
  ABSTRACT  
 
No abstract given.

 
  Selected figure(s)  
 
Figure 1.
Figure 1. A, Domain structure of spinophilin (top) and neurabin (bottom). Sequence identity between the domains is annotated in the figure. B, Primary sequence alignment of the neurabin SAM and shank3 SAM domains. The zinc binding residues in shank3 and the corresponding residues in neurabin are highlighted by boxes (see text). The shank3 (M1803E) mutation that is necessary to achieve high enough protein solubility and reduced aggregation is underlined. Secondary structure for the neurabin SAM domain is included above the sequence alignment.
Figure 2.
Figure 2. A, Stereo view of the bundle of 20 energy-minimized CYANA conformers representing the structure of neurabin[986-1056] (PDB ID 2GLE). The superposition is the best fit of the backbone atoms N, C^ , C of residues 4-70. Side chains with low local RMSD (<0.7) within the bundle are shown in cyan. Side chains of residues with high local RMSD (>0.7) are shown in green. Backbones are shown in dark blue. Aromatic heavy side chains are colored in orange. The local RMSD of Trp7, Trp15, Tyr24, and Phe28 are 0.31, 0.11, 0.87, and 0.62, respectively. B, Electrostatic surface of the neurabin SAM domain (left) and 180° rotation around x-axes (right). Red represents negative charges and blue positive charges. C, Ribbon presentation of the closest conformer to the mean coordinates of the bundle of 20 conformers used to represent the NMR structure of the neurabin SAM (left) and the shank3 SAM domain (right). The regular secondary structure elements are identified.
 
  The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2007, 69, 192-198) copyright 2007.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20712620 B.Pudelski, S.Kraus, J.Soll, and K.Philippar (2010).
The plant PRAT proteins - preprotein and amino acid transport in mitochondria and chloroplasts.
  Plant Biol (Stuttg), 12, 42-55.  
18618697 A.Bhunia, P.N.Domadia, H.Mohanram, and S.Bhattacharjya (2009).
NMR structural studies of the Ste11 SAM domain in the dodecyl phosphocholine micelle.
  Proteins, 74, 328-343.  
  18028445 H.Schüler, and W.Peti (2008).
Structure-function analysis of the filamentous actin binding domain of the neuronal scaffolding protein spinophilin.
  FEBS J, 275, 59-68.  
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.