PDBsum entry 1wn0

Signaling protein

PDB id: 1wn0

Contents

Protein chains

131 a.a. *

124 a.a. *

138 a.a. *

Waters ×103

* Residue conservation analysis

PDB id:

1wn0

Name:

Signaling protein

Title:

Crystal structure of histidine-containing phosphotransfer protein, zmhp2, from maize

Structure:

Histidine-containing phosphotransfer protein. Chain: a, b, c, d. Engineered: yes

Source:

Zea mays. Organism_taxid: 4577. Gene: zmhp2. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.20Å R-factor: 0.211 R-free: 0.248

Authors:

H.Sugawara,Y.Kawano,T.Hatakeyama,T.Yamaya,N.Kamiya,H.Sakakibara,Riken Structural Genomics/proteomics Initiative (Rsgi)

Key ref:

H.Sugawara et al. (2005). Crystal structure of the histidine-containing phosphotransfer protein ZmHP2 from maize. Protein Sci, 14, 202-208. PubMed id: 15576555 DOI: 10.1110/ps.041076905

Date:

24-Jul-04 Release date: 25-Jan-05

Protein chain

Q9SLX1  (Q9SLX1_MAIZE) -  Histidine-containing phosphotransfer protein from Zea mays

Seq: 145 a.a.

Struc: 131 a.a.

Protein chain

Q9SLX1  (Q9SLX1_MAIZE) -  Histidine-containing phosphotransfer protein from Zea mays

Seq: 145 a.a.

Struc: 124 a.a.

Protein chains

Q9SLX1  (Q9SLX1_MAIZE) -  Histidine-containing phosphotransfer protein from Zea mays

Seq: 145 a.a.

Struc: 138 a.a.

Enzyme reactions

• Enzyme class: Chains A, B, C, D: E.C.?

DOI no: 10.1110/ps.041076905

Protein Sci 14:202-208 (2005)

PubMed id: 15576555

Crystal structure of the histidine-containing phosphotransfer protein ZmHP2 from maize.

H.Sugawara, Y.Kawano, T.Hatakeyama, T.Yamaya, N.Kamiya, H.Sakakibara.

ABSTRACT

In higher plants, histidine-aspartate phosphorelays (two-component system) are involved in hormone signaling and stress responses. In these systems, histidine-containing phosphotransfer (HPt) proteins mediate the signal transmission from sensory histidine kinases to response regulators, including integration of several signaling pathways or branching into different pathways. We have determined the crystal structure of a maize HPt protein, ZmHP2, at 2.2 A resolution. ZmHP2 has six alpha-helices with a four-helix bundle at the C-terminus, a feature commonly found in HPt domains. In ZmHP2, almost all of the conserved residues among plant HPt proteins surround this histidine, probably forming the docking interface for the receiver domain of histidine kinase or the response regulator. Arg102 of ZmHP2 is conserved as a basic residue in plant HPt proteins. In bacteria, it is replaced by glutamine or glutamate that form a hydrogen bond to Ndelta atoms of the phospho-accepting histidine. It may play a key role in the complex formation of ZmHP2 with receiver domains.

Selected figure(s)

Figure 3.
Figure 3. Superimposition of active site structures of ZmHP2 and YPD1. Helices D and E, their connecting loops of ZmHP2 (all in purple), and the corresponding regions of YPD1 (pink) are shown. Oxygen, nitrogen, and sulfur atoms of selected residues are shown in red, blue, and green, respectively. Hydrogen bonds and salt bridges are indicated by dots.

Figure 5.
Figure 5. Structural differences between ZmHP2 molecules in the asymmetric unit around the loop connecting the four-helix bundle with the N-terminal helices. Compared to Figure 1 Go-, this figure is rotated by 90 degrees around the horizontal axis. Since the structures of the monomers of each pair of ZmHP2 molecules in the asymmetric unit are essentially the same, only molecules A1 (green) and B1 (purple) are shown. Oxygen, nitrogen and sulfur atoms are shown in red, blue and green, respectively. Hydrogen bonds and salt bridges are indicated by dots. In molecule A1, residues 35-38 are indicated in yellow. Gly41 in molecule A1 and three glycine residues (37, 38, and 41) in molecule B1 are colored pink. The residues of molecule A1 involved in packing interactions with molecule B1 in the crystal are shown in cyan.

The above figures are reprinted by permission from the Protein Society: Protein Sci (2005, 14, 202-208) copyright 2005.

Figures were selected by an automated process.