Unknown

Dataset Information

0

Structure of the hypothetical DUF1811-family protein GK0453 from Geobacillus kaustophilus HTA426.


ABSTRACT: The crystal structure of a conserved hypothetical protein, GK0453, from Geobacillus kaustophilus has been determined to 2.2 Å resolution. The crystal belonged to space group P4(3)2(1)2, with unit-cell parameters a = b = 75.69, c = 64.18 Å. The structure was determined by the molecular-replacement method and was refined to a final R factor of 22.6% (R(free) = 26.3%). Based on structural homology, the GK0453 protein possesses two independent binding sites and hence it may simultaneously interact with two proteins or with a protein and a nucleic acid.

SUBMITTER: Padmanabhan B 

PROVIDER: S-EPMC3614154 | biostudies-literature | 2013 Apr

REPOSITORIES: biostudies-literature

altmetric image

Publications

Structure of the hypothetical DUF1811-family protein GK0453 from Geobacillus kaustophilus HTA426.

Padmanabhan Balasundaram B   Nakamura Yoshihiro Y   Antonyuk Svetlana V SV   Strange Richard W RW   Hasnain S Samar SS   Yokoyama Shigeyuki S   Bessho Yoshitaka Y  

Acta crystallographica. Section F, Structural biology and crystallization communications 20130328 Pt 4


The crystal structure of a conserved hypothetical protein, GK0453, from Geobacillus kaustophilus has been determined to 2.2 Å resolution. The crystal belonged to space group P4(3)2(1)2, with unit-cell parameters a = b = 75.69, c = 64.18 Å. The structure was determined by the molecular-replacement method and was refined to a final R factor of 22.6% (R(free) = 26.3%). Based on structural homology, the GK0453 protein possesses two independent binding sites and hence it may simultaneously interact w  ...[more]

Similar Datasets

| PRJNA13233 | ENA
| S-EPMC3753961 | biostudies-literature
| S-EPMC3457123 | biostudies-literature
| S-EPMC8024623 | biostudies-literature
| S-EPMC2681792 | biostudies-literature
| S-EPMC4338136 | biostudies-literature
| S-EPMC4592879 | biostudies-literature
| S-EPMC10867098 | biostudies-literature
| PRJNA36721 | ENA
| PRJDB16840 | ENA