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Title: The structure of SAV1646 from Staphylococcus aureus belonging to a new ;ribosome-associated; subfamily of bacterial proteins

Authors:
; ; ; ; ; ; ; ; ; ;  [1];  [2];  [2];  [2]
  1. (Russ. Acad. Sci.)
  2. (
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
FOREIGN
OSTI Identifier:
1169361
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallogr. D; Journal Volume: 71; Journal Issue: (2) ; 02, 2015
Country of Publication:
United States
Language:
ENGLISH

Citation Formats

Chirgadze, Yuri N., Clarke, Teresa E., Romanov, Vladimir, Kisselman, Gera, Wu-Brown, Jean, Soloveychik, Maria, Chan, Tiffany S.Y., Gordon, Roni D., Battaile, Kevin P., Pai, Emil F., Chirgadze, Nickolay Y., Toronto), UHN), and HWMRI). The structure of SAV1646 from Staphylococcus aureus belonging to a new ;ribosome-associated; subfamily of bacterial proteins. United States: N. p., 2015. Web. doi:10.1107/S1399004714025619.
Chirgadze, Yuri N., Clarke, Teresa E., Romanov, Vladimir, Kisselman, Gera, Wu-Brown, Jean, Soloveychik, Maria, Chan, Tiffany S.Y., Gordon, Roni D., Battaile, Kevin P., Pai, Emil F., Chirgadze, Nickolay Y., Toronto), UHN), & HWMRI). The structure of SAV1646 from Staphylococcus aureus belonging to a new ;ribosome-associated; subfamily of bacterial proteins. United States. doi:10.1107/S1399004714025619.
Chirgadze, Yuri N., Clarke, Teresa E., Romanov, Vladimir, Kisselman, Gera, Wu-Brown, Jean, Soloveychik, Maria, Chan, Tiffany S.Y., Gordon, Roni D., Battaile, Kevin P., Pai, Emil F., Chirgadze, Nickolay Y., Toronto), UHN), and HWMRI). Sun . "The structure of SAV1646 from Staphylococcus aureus belonging to a new ;ribosome-associated; subfamily of bacterial proteins". United States. doi:10.1107/S1399004714025619.
@article{osti_1169361,
title = {The structure of SAV1646 from Staphylococcus aureus belonging to a new ;ribosome-associated; subfamily of bacterial proteins},
author = {Chirgadze, Yuri N. and Clarke, Teresa E. and Romanov, Vladimir and Kisselman, Gera and Wu-Brown, Jean and Soloveychik, Maria and Chan, Tiffany S.Y. and Gordon, Roni D. and Battaile, Kevin P. and Pai, Emil F. and Chirgadze, Nickolay Y. and Toronto) and UHN) and HWMRI)},
abstractNote = {},
doi = {10.1107/S1399004714025619},
journal = {Acta Crystallogr. D},
number = (2) ; 02, 2015,
volume = 71,
place = {United States},
year = {Sun Feb 01 00:00:00 EST 2015},
month = {Sun Feb 01 00:00:00 EST 2015}
}
  • The crystal structures of protein SA0856 from Staphylococcus aureus in its apo-form and in complex with a Zn2+-ion have been presented. The 152 amino acid protein consists of two similar domains with α + β topology. In both crystalline state and in solution, the protein forms a dimer with monomers related by a twofold pseudo-symmetry rotation axis. A sequence homology search identified the protein as a member of the structural family Glyoxalase I. We have shown that the enzyme possesses glyoxalase I activity in the presence of Zn2+, Mg2+, Ni2+, and Co2+, in this order of preference. Sequence and structuremore » comparisons revealed that human glyoxalase I should be assigned to a subfamily A, while S. aureus glyoxalase I represents a new subfamily B, which includes also proteins from other bacteria. Both subfamilies have a similar protein chain fold but rather diverse sequences. The active sites of human and staphylococcus glyoxalases I are also different: the former contains one Zn-ion per chain; the latter incorporates two of these ions. In the active site of SA0856, the first Zn-ion is well coordinated by His58, Glu60 from basic molecule and Glu40*, His44* from adjacent symmetry-related molecule. The second Zn3-ion is coordinated only by residue His143 from protein molecule and one acetate ion. We suggest that only single Zn1-ion plays the role of catalytic center. The newly found differences between the two subfamilies could guide the design of new drugs against S. aureus, an important pathogenic micro-organism.« less
  • No abstract prepared.
  • The Eap (extracellular adherence protein) of Staphylococcus aureus functions as a secreted virulence factor by mediating interactions between the bacterial cell surface and several extracellular host proteins. Eap proteins from different Staphylococcal strains consist of four to six tandem repeats of a structurally uncharacterized domain (EAP domain). We have determined the three-dimensional structures of three different EAP domains to 1.8, 2.2, and 1.35 {angstrom} resolution, respectively. These structures reveal a core fold that is comprised of an {alpha}-helix lying diagonally across a five-stranded, mixed {beta}-sheet. Comparison of EAP domains with known structures reveals an unexpected homology with the C-terminal domainmore » of bacterial superantigens. Examination of the structure of the superantigen SEC2 bound to the {beta}-chain of a T-cell receptor suggests a possible ligand-binding site within the EAP domain (Fields, B. A., Malchiodi, E. L., Li, H., Ysern, X., Stauffacher, C. V., Schlievert, P. M., Karjalainen, K., and Mariuzza, R. (1996) Nature 384, 188-192). These results provide the first structural characterization of EAP domains, relate EAP domains to a large class of bacterial toxins, and will guide the design of future experiments to analyze EAP domain structure/function relationships.« less
  • Ebh, a giant protein found in staphylococci, contains several domains, including a large central region with 52 imperfect repeats of a domain composed of 126 amino acids. We used electron microscopy to observe the rod-like structure of a partial Ebh protein containing 10 repeating units. This is the first report of the direct observation of an Ebh structure containing a large number of repeating units, although structures containing one, two, or four repeating units have been reported. The observed structure of the partial Ebh protein was distorted and had a length of ca. 520 A and a width of ca.more » 21 A. The observed structures were consistent with those deduced from crystal structure analysis, suggesting that the Ebh domains are connected to form a rod-like structure. The crystal structure data revealed distorted, string-like features in the simulated structure of the whole-length Ebh protein. Superposition of fragments of the simulated whole-length structure of the Ebh protein onto each electron micrograph showed a high level of correlation between the observed and calculated structures. These results suggest that Ebh is composed of highly flexible filate molecules. The highly repetitive structure and the associated unique structural flexibility of Ebh support the proposed function of this protein, i.e. binding to sugars in the cell wall. This binding might result in intra-cell-wall cross-linking that contributes to the rigidity of bacterial cells.« less