PDBsum entry: 1no5

Structural genomics, unknown function

PDB id: 1no5

Contents

Protein chains

100 a.a. *

Ligands

GOL

SO4 ×2

Metals

_NA

_ZN ×8

Waters ×304

* Residue conservation analysis

PDB id:

1no5

Name:

Structural genomics, unknown function

Title:

Structure of hi0073 from haemophilus influenzae, the nucleot binding domain of the hi0073/hi0074 two protein nucleotidyl transferase.

Structure:

Hypothetical protein hi0073. Chain: a, b. Engineered: yes

Source:

Haemophilus influenzae. Organism_taxid: 727. Gene: hi0073. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.80Å R-factor: 0.201 R-free: 0.282

Authors:

C.Lehmann,S.Pullalarevu,A.Galkin,W.Krajewski,M.A.Willis,A.Ho O.Herzberg,Structure 2 Function Project (S2f)

Key ref:

C.Lehmann et al. (2005). Structure of HI0073 from Haemophilus influenzae, the nucleotide-binding domain of a two-protein nucleotidyl transferase. Proteins, 60, 807-811. PubMed id: 16028221 DOI: 10.1002/prot.20586

Date:

15-Jan-03 Release date: 16-Mar-04

Protein chains

P43933  (Y073_HAEIN) -  Uncharacterized protein HI_0073

Seq: 114 a.a.

Struc: 100 a.a.

 Gene Ontology (GO) functional annotation 

• Biochemical function: nucleotidyltransferase activity (1 term)

DOI no: 10.1002/prot.20586

Proteins 60:807-811 (2005)

PubMed id: 16028221

Structure of HI0073 from Haemophilus influenzae, the nucleotide-binding domain of a two-protein nucleotidyl transferase.

C.Lehmann, S.Pullalarevu, W.Krajewski, M.A.Willis, A.Galkin, A.Howard, O.Herzberg.

ABSTRACT

No abstract given.

Selected figure(s)

Figure 1.
Figure 1. Structure and nucleotide binding of HI0073. (A) Ribbon diagram of the fold. -helices are colored in salmon-red; -strands are colored in lilac. The N- and C-termini are labeled. (B) Stereoscopic view of the binuclear metal binding site. The aspartic acids (Asp46, Asp48, and Asp79) that serve as ligands to the metal, as well as the glutamic acids from the symmetry-related molecule (Glu67 and Glu71 ), are shown as a stick model with the following color scheme: oxygen, red; carbon, green. Zinc ions are shown as gold spheres, and water molecules as red spheres. The loop following 1 is highlighted in dark salmon-red. Shown in a gold stick model is DCT from the structure of the DNA polymerase complex. Its position was obtained by superposing the binuclear metal cluster and the 2 aspartic acids common to the 2 enzymes. (C) Progress curve of TTP titration. Tryptophan fluorescence energy transfer is provided as a function of TTP concentration. The data were fitted to a hyperbolic function to obtain a K[d] value of 72 ± 5 M.

The above figure is reprinted by permission from John Wiley & Sons, Inc.: Proteins (2005, 60, 807-811) copyright 2005.