Unknown

Dataset Information

0

The crystal structure of Aq_328 from the hyperthermophilic bacteria Aquifex aeolicus shows an ancestral histone fold.


ABSTRACT: The structure of Aq_328, an uncharacterized protein from hyperthermophilic bacteria Aquifex aeolicus, has been determined to 1.9 A by using multi-wavelength anomalous diffraction (MAD) phasing. Although the amino acid sequence analysis shows that Aq_328 has no significant similarity to proteins with a known structure and function, the structure comparison by using the Dali server reveals that it: (1) assumes a histone-like fold, and (2) is similar to an ancestral nuclear histone protein (PDB code 1F1E) with z-score 8.1 and RMSD 3.6 A over 124 residues. A sedimentation equilibrium experiment indicates that Aq_328 is a monomer in solution, with an average sedimentation coefficient of 2.4 and an apparent molecular weight of about 20 kDa. The overall architecture of Aq_328 consists of two noncanonical histone domains in tandem repeat within a single chain, and is similar to eukaryotic heterodimer (H2A/H2B and H3/H4) and an archaeal histone heterodimer (HMfA/HMfB). The sequence comparisons between the two histone domains of Aq_328 and six eukaryotic/archaeal histones demonstrate that most of the conserved residues that underlie the Aq_328 architecture are used to build and stabilize the two cross-shaped antiparallel histone domains. The high percentage of salt bridges in the structure could be a factor in the protein's thermostability. The structural similarities to other histone-like proteins, molecular properties, and potential function of Aq_328 are discussed in this paper.

SUBMITTER: Qiu Y 

PROVIDER: S-EPMC2792020 | biostudies-literature | 2006 Jan

REPOSITORIES: biostudies-literature

altmetric image

Publications

The crystal structure of Aq_328 from the hyperthermophilic bacteria Aquifex aeolicus shows an ancestral histone fold.

Qiu Yang Y   Tereshko Valentina V   Kim Youngchang Y   Zhang Rongguang R   Collart Frank F   Yousef Mohammed M   Kossiakoff Anthony A   Joachimiak Andrzej A  

Proteins 20060101 1


The structure of Aq_328, an uncharacterized protein from hyperthermophilic bacteria Aquifex aeolicus, has been determined to 1.9 A by using multi-wavelength anomalous diffraction (MAD) phasing. Although the amino acid sequence analysis shows that Aq_328 has no significant similarity to proteins with a known structure and function, the structure comparison by using the Dali server reveals that it: (1) assumes a histone-like fold, and (2) is similar to an ancestral nuclear histone protein (PDB cod  ...[more]

Similar Datasets

| S-EPMC1079890 | biostudies-literature
| S-EPMC123006 | biostudies-literature
| S-EPMC1151740 | biostudies-literature
| PRJNA35137 | ENA
| S-EPMC2676054 | biostudies-literature
| S-EPMC2335016 | biostudies-literature
| S-EPMC1142543 | biostudies-literature
| PRJNA215 | ENA
| S-EPMC2496870 | biostudies-literature
| S-EPMC4125815 | biostudies-literature