 |
PDBsum entry 3e56
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Unknown function
|
PDB id
|
|
|
|
3e56
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Crystal structure of npun_r1517, A putative negative regulator of heterocyst differentiation from nostoc punctiforme pcc 73102.
|
|
|
Authors
|
|
S.Ni,
M.M.Benning,
M.J.Smola,
E.A.Feldmann,
M.A.Kennedy.
|
|
|
Ref.
|
|
Proteins, 2009,
74,
794-798.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
No abstract given.
|
|
|
|
|
|
|
|
Figure 1.
Figure 1. (A) A ribbon representation of the fold of the
Npun_R1517 monomer. The elements of secondary structure are
indicated, as well as the position of the N- and C-termini. (B)
A ribbon representation of the homodimer of Npun_R1517 looking
down onto the two symmetry-related  2
helices. The dimer is formed by a symmetry operation belonging
to the P4[3]2[1]2 space group as described in the text. (C) The
same dimer as shown in (B) rotated by 90° along the long
axis of the dimer. All hydrophobic residues including L, I, V,
and F are represented as sticks to illustrated how the
hydrophobic core is formed between each 2
helix and hydrophobic residues from  -strands
of both chains, as described in the text. (D) A zoomed-in
illustration of the position of the nest residues, E51, G52, and
S53 (represented as sticks color-coded by atom type), as well as
the location of the R84 and R86 (represented as sticks colored
red).
|
|
Figure 2.
Figure 2. (A) The electrostatic potential surface of Npun_R1517
looking down onto the two symmetry-related 2
helices. The locations of key residues discussed in the text are
indicated by arrows. (B) The electrostatic potential surface of
Npun_R1517 looking down onto the four-stranded antiparallel -sheet.
The electrostatic potential surface, which was generated using
the APBS module within MacPyMOL (DeLano Scientific, 2006),
ranges from -5 kT (red) to 5 kT (blue).
|
|
|
|
|
|
The above figures are
reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2009,
74,
794-798)
copyright 2009.
|
|
|
|
|
|
|
