PDBsum entry 1kpc

Protein kinasE C interacting protein

PDB id: 1kpc

Contents

Protein chain

111 a.a. *

Waters ×294

* Residue conservation analysis

PDB id:

1kpc

Name:

Protein kinasE C interacting protein

Title:

Pkci-1-apo+zinc

Structure:

Human protein kinasE C interacting protein 1 (zinc protein). Chain: a, b, c, d. Synonym: pkci-1, protein kinasE C inhibitor 1. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: hpkci-1. Expressed in: pichia pastoris. Expression_system_taxid: 4922. Other_details: expressed as an acetylated protein on amino acid 2. This is similar to the native protein purified directly from bovine brain.

Biol. unit:

Dimer (from PQS)

Resolution:

2.20Å R-factor: 0.217 R-free: 0.309

Authors:

C.D.Lima,M.G.Klein,I.B.Weinstein,W.A.Hendrickson

Key ref:

C.D.Lima et al. (1996). Three-dimensional structure of human protein kinase C interacting protein 1, a member of the HIT family of proteins. Proc Natl Acad Sci U S A, 93, 5357-5362. PubMed id: 8643579

Date:

06-Jan-96 Release date: 11-Jul-96

Protein chains

P49773  (HINT1_HUMAN) -  Adenosine 5'-monophosphoramidase HINT1 from Homo sapiens

Seq: 126 a.a.

Struc: 111 a.a.

Enzyme reactions

• Enzyme class 2: E.C.3.4.22.- - ?????
• Enzyme class 3: E.C.3.9.1.- - ?????

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Proc Natl Acad Sci U S A 93:5357-5362 (1996)

PubMed id: 8643579

Three-dimensional structure of human protein kinase C interacting protein 1, a member of the HIT family of proteins.

C.D.Lima, M.G.Klein, I.B.Weinstein, W.A.Hendrickson.

ABSTRACT

The three-dimensional structure of protein kinase C interacting protein 1 (PKCI-1) has been solved to high resolution by x-ray crystallography using single isomorphous replacement with anomalous scattering. The gene encoding human PKCI-1 was cloned from a cDNA library by using a partial sequence obtained from interactions identified in the yeast two-hybrid system between PKCI-1 and the regulatory domain of protein kinase C-beta. The PKCI-1 protein was expressed in Pichia pastoris as a dimer of two 13.7-kDa polypeptides. PKCI-1 is a member of the HIT family of proteins, shown by sequence identity to be conserved in a broad range of organisms including mycoplasma, plants, and humans. Despite the ubiquity of this protein sequence in nature, no distinct function has been shown for the protein product in vitro or in vivo. The PKCI-1 protomer has an alpha+beta meander fold containing a five-stranded antiparallel sheet and two helices. Two protomers come together to form a 10-stranded antiparallel sheet with extensive contacts between a helix and carboxy terminal amino acids of a protomer with the corresponding amino acids in the other protomer. PKCI-1 has been shown to interact specifically with zinc. The three-dimensional structure has been solved in the presence and absence of zinc and in two crystal forms. The structure of human PKCI-1 provides a model of this family of proteins which suggests a stable fold conserved throughout nature.