PDBsum entry 1n4t

Hydrolase

PDB id: 1n4t

Contents

Protein chain

219 a.a.

Obsolete entry

PDB id:

1n4t

Name:

Hydrolase

Title:

Solution structure of the catalytic domain from rat cnp

Structure:

2',3'-cyclic nucleotide 3'-phosphodiesterase. Chain: a. Fragment: catalytic domain (residues 184-398). Engineered: yes

Source:

Rattus norvegicus. Rat. Gene: cnp1. Expressed in: escherichia coli.

NMR struc:

20 models

Authors:

G.Kozlov,J.Lee,P.Gutierrez,I.Ekiel,P.E.Braun,K.Gehring

Key ref:

G.I.Lee et al. (2003). NMR structure of the forkhead-associated domain from the Arabidopsis receptor kinase-associated protein phosphatase. Proc Natl Acad Sci U S A, 100, 11261-11266. PubMed id: 14500786 DOI: 10.1073/pnas.2031918100

Date:

01-Nov-02 Release date: 09-Sep-03

Protein chain

P13233  (CN37_RAT) -  2',3'-cyclic-nucleotide 3'-phosphodiesterase from Rattus norvegicus

Seq: 420 a.a.

Struc: 219 a.a.*

* PDB and UniProt seqs differ at 4 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.3.1.4.37 - 2',3'-cyclic-nucleotide 3'-phosphodiesterase.
• Reaction: a nucleoside 2',3'-cyclic phosphate + H2O = a nucleoside 2'-phosphate + H⁺

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

DOI no: 10.1073/pnas.2031918100

Proc Natl Acad Sci U S A 100:11261-11266 (2003)

PubMed id: 14500786

NMR structure of the forkhead-associated domain from the Arabidopsis receptor kinase-associated protein phosphatase.

G.I.Lee, Z.Ding, J.C.Walker, S.R.Van Doren.

ABSTRACT

Forkhead-associated (FHA) domains are phosphoprotein-binding modules found in diverse signaling proteins that bind partners phosphorylated on threonine or serine. Kinase-associated protein phosphatase from Arabidopsis employs its FHA domain for negative regulation of receptor-like kinase signaling pathways, which are important in plant development. The solution structure of the free state of kinase-interacting FHA domain (KI-FHA) of kinase-associated protein phosphatase has been determined with high precision and accuracy using residual dipolar couplings. KI-FHA is a sandwich of a five-stranded mixed beta-sheet with a six-stranded antiparallel beta-sheet. Despite homology only in the recognition loops, this fold is shared with FHA domains from checkpoint proteins from yeast and humans, as well as with nonhomologous MH2 domains of Smad tumor suppressors. A shared pattern of hydrophobicity throughout FHA domains and Smad MH2 domains may stabilize the core of the beta-sandwich. Evolutionary trace analysis of FHA domains suggests class-specific residues in the recognition loops that could tune their phosphoprotein-binding specificity. This surface agrees with that of KI-FHA in contact with a phosphothreonine peptide ligand. Evolutionary trace analysis also predicts an unexpected swath of class-specific residues on another face of FHA domains. Protein interactions with these faces may affect assembly of transmembrane signaling complexes in plants, and in other FHA domain-containing assemblies.

Selected figure(s)

Figure 3.
Fig. 3. Phosphoprotein-binding surface of KI-FHA (a, b, and c) and of FHA2 of RAD53 (d). (a) The class-specific residues at trace level 9 are blue. (Fig. 6 summarizes the alignment of class consensus residues at trace level 9.) The residues identical among KAPP of maize, rice, and Arabidopsis are yellow in a.(b) KI-FHA residues with amide NMR peaks most shifted by saturating amounts of the pThr peptide from BAK1 (2 mM peptide:0.5 mM KI-FHA); i.e., with [HN] > 0.16 ppm are red. Those residues with 0.16 ppm > [HN] > 0.06 ppm are pink. Surface properties of KI-FHA (c) and RAD53 FHA2 (d) are yellow for hydrophobic, blue for positively charged, and red for negatively charged residues.

Figure 4.
Fig. 4. Unexpected class-specific surface suggests another interaction surface. This view is rotated 90° about the x axis relative to Fig. 3, placing the six-stranded -sheet in the foreground. The color code is the same as that of Fig. 3a. (a) The CPK surface. (b) A backbone ribbon of KI-FHA in the same orientation as a.

Figures were selected by an automated process.