PDBsum entry 2fqh

Structural genomics, unknown function

PDB id: 2fqh

Contents

Protein chain

109 a.a. *

* Residue conservation analysis

PDB id:

2fqh

Name:

Structural genomics, unknown function

Title:

Nmr structure of hypothetical protein ta0938 from termoplasma acidophilum

Structure:

Hypothetical protein ta0938. Chain: a. Engineered: yes

Source:

Thermoplasma acidophilum. Organism_taxid: 2303. Expressed in: escherichia coli. Expression_system_taxid: 562

NMR struc:

20 models

Authors:

D.Monleon,V.Esteve,A.Yee,C.Arrowsmith,B.Celda,Ontario Centre For Structural Proteomics (Ocsp)

Key ref:

D.Monleón et al. (2007). NMR structure of hypothetical protein TA0938 from Thermoplasma acidophilum. Proteins, 67, 1185-1188. PubMed id: 17377985 DOI: 10.1002/prot.21143

Date:

18-Jan-06 Release date: 09-Jan-07

Protein chain

Q9HJM9  (Q9HJM9_THEAC) -  C2H2-type domain-containing protein from Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)

Seq: 110 a.a.

Struc: 109 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1002/prot.21143

Proteins 67:1185-1188 (2007)

PubMed id: 17377985

NMR structure of hypothetical protein TA0938 from Thermoplasma acidophilum.

D.Monleón, A.Yee, C.Arrowsmith, B.Celda.

ABSTRACT

No abstract given.

Selected figure(s)

Figure 1.
Figure 1. NMR solution structure of TA0938. A. Stereo view of the superposition of the final 20 structures over the average NMR structure. B. Ribbon diagram depicting lowest target function NMR structure of TA0938 of Thermoplasma acidophillum (PDB accession code 2FQH). The -helices are shown in red and yellow and -sheets are shown in cyan. Side-chains of cysteine residues are shown in blue. Chemical shift values for cysteines C in TA0938 were: Cys20, 44.14 ppm; Cys23, 32.28 ppm; Cys42, 36.02 ppm; Cys43, 34.36 ppm; and Cys46 43.10 ppm C. Sausage presentation of backbone of TA0938. Thickness of the cylindrical rod is proportional to the mean of the global displacements of the C atoms in the 20 DYANA best conformers. The -strands are shown in green, the -helices in red and cysteine residues in yellow.

Figure 2.
Figure 2. A. Comparison between cysteine-enriched regions of TA0938 (in red) and E. Coli CLPX chaperone Zinc binding domain dimer (PDB code 1OVX, in blue). B. Sequence alignment of TA0938, closest homologues hypothetical proteins Q97VD3_SULSO and Q96XA7_SULTO and cysteine-rich segment from Escherichia coli CLPX chaperone Zinc binding domain. Secondary structure elements in TA0938 structure have been plotted in the sequence. Cysteines have been marked inside a rectangle.

The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2007, 67, 1185-1188) copyright 2007.