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PDBsum entry 1os3

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protein metals Protein-protein interface(s) links
Hormone/growth factor PDB id
1os3
Jmol
Contents
Protein chains
21 a.a.
29 a.a. *
28 a.a. *
Metals
_CL ×2
_ZN ×2
Waters ×40
* Residue conservation analysis
PDB id:
1os3
Name: Hormone/growth factor
Title: Dehydrated t6 human insulin at 100 k
Structure: Insulin. Chain: a, c. Fragment: a-chain. Insulin. Chain: b, d. Fragment: b-chain
Source: Homo sapiens. Human. Organism_taxid: 9606. Organism_taxid: 9606
Resolution:
1.95Å     R-factor:   0.216     R-free:   0.253
Authors: G.D.Smith,R.H.Blessing
Key ref:
G.D.Smith and R.H.Blessing (2003). Lessons from an aged, dried crystal of T(6) human insulin. Acta Crystallogr D Biol Crystallogr, 59, 1384-1394. PubMed id: 12876340 DOI: 10.1107/S090744490301165X
Date:
18-Mar-03     Release date:   29-Jul-03    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P01308  (INS_HUMAN) -  Insulin
Seq:
Struc:
110 a.a.
21 a.a.
Protein chain
Pfam   ArchSchema ?
P01308  (INS_HUMAN) -  Insulin
Seq:
Struc:
110 a.a.
29 a.a.
Protein chain
Pfam   ArchSchema ?
P01308  (INS_HUMAN) -  Insulin
Seq:
Struc:
110 a.a.
28 a.a.
Key:    PfamA domain  Secondary structure

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   1 term 
  Biochemical function     hormone activity     1 term  

 

 
DOI no: 10.1107/S090744490301165X Acta Crystallogr D Biol Crystallogr 59:1384-1394 (2003)
PubMed id: 12876340  
 
 
Lessons from an aged, dried crystal of T(6) human insulin.
G.D.Smith, R.H.Blessing.
 
  ABSTRACT  
 
The structure of the T(6) hexameric form of human insulin has been determined at both room temperature and 100 K from a single air-dried crystal. At 100 K, the space group is R3 and the asymmetric unit consists of a dimer, as has been observed previously in hydrated structures. At room temperature, the space group is P1 and the unit cell contains a quasi-threefold-symmetric hexamer. In the absence of stabilizing water interactions, the N-termini of all six A chains in the room-temperature structure appear to have undergone partial unfolding, but the N-termini of these chains are well ordered in the 100 K structure. Other differences between the room-temperature and 100 K structures involve the coordination around the zinc ions. At 100 K, both zinc ions clearly exhibit dual coordination: zinc is octahedrally coordinated in one half of the zinc sites but tetrahedrally coordinated in the other half; at room temperature, the electron densities suggest tetrahedral coordination but the bond distances to the fourth ligands are longer than expected. Contrary to what has been observed to date in all other T(6) insulin structures, there are no contacts between pairs of GluB13 residues, either at room temperature or at 100 K, that would suggest the presence of a hydrogen bond. At room temperature, three of the six independent GluB13 side chains are disordered; at 100 K, both independent side chains are disordered. The disorder in the GluB13 side chains and the lack of contacts between carboxylate groups suggests that as a result of disruption of the hydration structure in the central core of the hexamer, all six B13 carboxylates bear a negative charge. This in turn suggests that in the hydrated structures the well ordered water structure in the central core is involved in stabilizing the B13 side-chain conformations and modulating charge repulsions among the six B13 glutamates if they are not protonated, or that, as is considered more likely, the water structure plays an important role in modulating the pK(a) values of the B13 glutamates, resulting in protonation and hydrogen-bond formation.
 
  Selected figure(s)  
 
Figure 7.
Figure 7 The 1 -contoured [A]-weighted (2F[o] - F[c]) electron density in the central core of the T[6] insulin hexamer in the rhombohedral structure of the dehydrated crystal at 100 K. The view is along the crystallographic threefold axis. The C^atoms (CG) are labeled on those GluB13 residues which are incomplete owing to disordered carboxylate groups. Prepared with the programs XtalView (McRee, 1999[McRee, C. E. (1999). J. Struct. Biol. 125, 156-165.]) and Raster3D (Merritt & Bacon, 1997[Merritt, E. A. & Bacon, D. J. (1997). Methods Enzymol. 277, 505-524.]).
Figure 8.
Figure 8 A schematic illustration of the packing of T[6] insulin hexamers in the hydrated R3 structure as viewed along the hexagonal c axis. Dashed lines denote the pseudo-twofold axes within the hexamers and the approximate boundary of each dimer. `A' and `B' label contact sites that contain five and six surface residues, respectively, that form nine interhexamer contacts of less than 3.4 , four of which are hydrogen bonds. Not shown are the contacts that exist between hexamers related by a translation along the c axis.
 
  The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2003, 59, 1384-1394) copyright 2003.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20697659 A.C.Welinder, J.Zhang, D.B.Steensgaard, and J.Ulstrup (2010).
Adsorption of human insulin on single-crystal gold surfaces investigated by in situ scanning tunnelling microscopy and electrochemistry.
  Phys Chem Chem Phys, 12, 9999.  
15965985 J.J.Hill, E.Y.Shalaev, and G.Zografi (2005).
Thermodynamic and dynamic factors involved in the stability of native protein structure in amorphous solids in relation to levels of hydration.
  J Pharm Sci, 94, 1636-1667.  
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