PDBsum entry 1ufd

Membrane protein

PDB id: 1ufd

Contents

Protein chains

215 a.a.

Theoretical model

PDB id:

1ufd

Name:

Membrane protein

Title:

Comparative modeling of nodulin 26 from glycine max.

Structure:

Nodulin 26. Chain: a, b, c, d. Fragment: residues 36-250

Source:

Glycine max. Soybean

Authors:

S.Biswas

Key ref:

S.Biswas (2004). Functional properties of soybean nodulin 26 from a comparative three-dimensional model. FEBS Lett, 558, 39-44. PubMed id: 14759513 DOI: 10.1016/S0014-5793(03)01529-1

Date:

28-May-03 Release date: 10-Feb-04

Protein chains

P08995  (NO26_SOYBN) -  Nodulin-26

Seq: 271 a.a.

Struc: 215 a.a.

DOI no: 10.1016/S0014-5793(03)01529-1

FEBS Lett 558:39-44 (2004)

PubMed id: 14759513

Functional properties of soybean nodulin 26 from a comparative three-dimensional model.

S.Biswas.

ABSTRACT

A model of the nodulin 26 channel protein has been constructed based on comparative modeling and molecular dynamics simulations. Structural features of the protein indicate a selectivity filter that differs from those of the known structures of Escherichia coli glycerol facilitator and mammalian aquaporin 1. The model structure also reveals important roles of Ser207 and Phe96 in ligand binding and transport.

Selected figure(s)

Figure 4.
Fig. 4. a: Interaction of second formamide molecule (CP2) with Ser207 when the first one (CP1) reaches at the constriction region. b: Two rotamer conformations, indicated by side chain torsion angle χ value of Ser207 during the 120 ps trajectory for four monomers A, B, C and D. Ser207 in monomers A and D changes their side chain conformation in the trajectory. χ[1] value near zero corresponds to the conformation of Ser207 when it interacts to ligand molecule at the region in between the selectivity filter and the constriction region.

Figure 5.
Fig. 5. Comparison of electrostatic potential surfaces of nodulin 26, GlpF and AQP1 at the extracellular face. The figure was generated by GRASP [30].

The above figures are reprinted by permission from the Federation of European Biochemical Societies: FEBS Lett (2004, 558, 39-44) copyright 2004.

Figures were selected by the author.