PDBsum entry 2zts

Atp-binding protein

PDB id: 2zts

Contents

Protein chains

216 a.a. *

Ligands

ADP ×3

Metals

_MG ×3

Waters ×88

* Residue conservation analysis

PDB id:

2zts

Name:

Atp-binding protein

Title:

Crystal structure of kaic-like protein ph0186 from hyperthermophilic archaea pyrococcus horikoshii ot3

Structure:

Putative uncharacterized protein ph0186. Chain: a, b, c. Engineered: yes

Source:

Pyrococcus horikoshii. Organism_taxid: 53953. Strain: ot3. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.07Å R-factor: 0.199 R-free: 0.250

Authors:

H.Ming,K.Miyazono,M.Tanokura

Key ref:

H.J.Kang et al. (2009). Crystal structure of KaiC-like protein PH0186 from hyperthermophilic archaea Pyrococcus horikoshii OT3. Proteins, 75, 1035-1039. PubMed id: 19274727 DOI: 10.1002/prot.22367

Date:

08-Oct-08 Release date: 24-Mar-09

Protein chains

O57925  (O57925_PYRHO) -  KaiC domain-containing protein from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)

Seq: 251 a.a.

Struc: 216 a.a.

DOI no: 10.1002/prot.22367

Proteins 75:1035-1039 (2009)

PubMed id: 19274727

Crystal structure of KaiC-like protein PH0186 from hyperthermophilic archaea Pyrococcus horikoshii OT3.

H.J.Kang, K.Kubota, H.Ming, K.Miyazono, M.Tanokura.

ABSTRACT

No abstract given.

Selected figure(s)

Figure 1.
Figure 1. Structure of PH0186. (A) Ribbon diagram of the monomer structure of PH0186. Color-coding runs from blue in the N-terminal region to red in the C-terminal region. Secondary structure assignments are labeled on the ribbon model. ADP molecules are presented by a stick model. Residues 99-117 and 183-186 are missing in the structure (shown by the dotted line). (B) The hexamer structure of PH0186. Subunits A(A ), B(B ), and C(C ) of the PH0186 hexamer are colored blue, purple, and orange, respectively. ADP molecules are presented by a stick model. The six-fold axis of the hexamer is presented by a black hexagon. (C) ADP binding manner in the hexamer structure of PH0186. Residues involved in ADP binding are presented by a stick model. The Mg^2+ ion is shown as a green ball near the phosphate group of ADP.

Figure 2.
Figure 2. Comparison with another structure. (A) Amino acid sequence alignment of PH0186 and KaiCI from Synechococcus sp. The secondary structure assignment for PH0186 is indicated by helices ( - and 3[10]-helices) and arrows ( -strands). Each protein contains Walker motifs A and B, and two catalytic carboxylate Glu residues. (B) Superposition of PH0186 (blue) and KaiCI (red). (C) The comparative electrostatic potential diagrams of PH0186 (a), and KaiCI (b). Positive and negative potentials are represented by blue and red, respectively. The maximum and the minimum values of electrostatic potentials are ±1 kT/e, respectively. Electrostatic potential of each protein was calculated using default parameters of APBS.

The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2009, 75, 1035-1039) copyright 2009.