PDBsum entry: 1jog

Structural genomics, unknown function

PDB id: 1jog

Contents

Protein chains

135 a.a. *

Waters ×140

* Residue conservation analysis

PDB id:

1jog

Name:

Structural genomics, unknown function

Title:

Structure of hi0074 from heamophilus influenzae reveals the fold of a substrate binding domain of a nucleotidyltransferase

Structure:

Hypothetical protein hi0074. Chain: a, b, c, d. Engineered: yes

Source:

Haemophilus influenzae. Organism_taxid: 727. Gene: hi0074. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Dimer (from PQS)

Resolution:

2.40Å R-factor: 0.211 R-free: 0.282

Authors:

C.Lehmann,K.Lim,O.Herzberg,Structure 2 Function Project (S2f)

Key ref:

C.Lehmann et al. (2003). The HI0073/HI0074 protein pair from Haemophilus influenzae is a member of a new nucleotidyltransferase family: structure, sequence analyses, and solution studies. Proteins, 50, 249-260. PubMed id: 12486719 DOI: 10.1002/prot.10260

Date:

29-Jul-01 Release date: 18-Dec-02

Protein chains

P43934  (Y074_HAEIN) -  Uncharacterized protein HI_0074

Seq: 146 a.a.

Struc: 135 a.a.

DOI no: 10.1002/prot.10260

Proteins 50:249-260 (2003)

PubMed id: 12486719

The HI0073/HI0074 protein pair from Haemophilus influenzae is a member of a new nucleotidyltransferase family: structure, sequence analyses, and solution studies.

C.Lehmann, K.Lim, V.R.Chalamasetty, W.Krajewski, E.Melamud, A.Galkin, A.Howard, Z.Kelman, P.T.Reddy, A.G.Murzin, O.Herzberg.

ABSTRACT

The crystal structure of HI0074 from Haemophilus influenzae, a protein of unknown function, has been determined at a resolution of 2.4 A. The molecules form an up-down, four-helix bundle, and associate into homodimers. The fold is most closely related to the substrate-binding domain of KNTase, yet the amino acid sequences of the two proteins exhibit no significant homology. Sequence analyses of completely and incompletely sequenced genomes reveal that the two adjacent genes, HI0074 and HI0073, and their close relatives comprise a new family of nucleotidyltransferases, with 15 members at the time of writing. The analyses also indicate that this is one of eight families of a large nucleotidyltransferase superfamily, whose members were identified based on the proximity of the nucleotide- and substrate-binding domains on the respective genomes. Both HI0073 and HI0074 were annotated "hypothetical" in the original genome sequencing publication. HI0073 was cloned, expressed, and purified, and was shown to form a complex with HI0074 by polyacrylamide gel electrophoresis under nondenaturing conditions, analytic size exclusion chromatography, and dynamic light scattering. Double- and single-stranded DNA binding assays showed no evidence of DNA binding to HI0074 or to HI0073/HI0074 complex despite the suggestive shape of the putative binding cleft formed by the HI0074 dimer.

Selected figure(s)

Figure 1.
Figure 1. Stereoscopic view of the electron density maps together with the final model. The coefficients (2F[o] - F[c]) and calculated phases are used. The map is sigma(a)-weighted[33] and contoured at 1 .

Figure 6.
Figure 6. Superposition of HI0074 (turquoise) and KNTase (yellow). The DALI orientation matrix was used for superposition.

The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2003, 50, 249-260) copyright 2003.

Figures were selected by an automated process.