PDBsum entry 3e56

Unknown function

PDB id: 3e56

Contents

Protein chain

75 a.a.

Waters ×59

PDB id:

3e56

Name:

Unknown function

Title:

The 2.0 angstrom resolution crystal structure of npr1517, a putative heterocyst differentiation inhibitor from nostoc punctiforme

Structure:

Putative uncharacterized protein. Chain: a. Fragment: unp residues 1-88. Engineered: yes

Source:

Nostoc punctiforme. Organism_taxid: 63737. Strain: pcc 73102. Gene: npun_r1517. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.01Å R-factor: 0.190 R-free: 0.237

Authors:

M.A.Kennedy,S.Ni,M.J.Smola

Key ref:

S.Ni et al. (2009). Crystal structure of Npun_R1517, a putative negative regulator of heterocyst differentiation from Nostoc punctiforme PCC 73102. Proteins, 74, 794-798. PubMed id: 19089958 DOI: 10.1002/prot.22308

Date:

13-Aug-08 Release date: 20-Jan-09

Protein chain

B2IZS7  (B2IZS7_NOSP7) -  Npun R1517 domain-containing protein from Nostoc punctiforme (strain ATCC 29133 / PCC 73102)

Seq: 94 a.a.

Struc: 75 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1002/prot.22308

Proteins 74:794-798 (2009)

PubMed id: 19089958

Crystal structure of Npun_R1517, a putative negative regulator of heterocyst differentiation from Nostoc punctiforme PCC 73102.

S.Ni, M.M.Benning, M.J.Smola, E.A.Feldmann, M.A.Kennedy.

ABSTRACT

No abstract given.

Selected figure(s)

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.