Menu
×
West Ashley Library
9 a.m. - 5 p.m.
Phone: (843) 766-6635
Wando Mount Pleasant Library
9 a.m. - 5 p.m.
Phone: (843) 805-6888
Village Library
9 a.m. - 1 p.m.
Phone: (843) 884-9741
St. Paul's/Hollywood Library
9 a.m. - 5 p.m.
Phone: (843) 889-3300
Otranto Road Library
9 a.m. - 5 p.m.
Phone: (843) 572-4094
Mt. Pleasant Library
9 a.m. – 5 p.m.
Phone: (843) 849-6161
McClellanville Library
9 a.m. – 1 p.m.
Phone: (843) 887-3699
Keith Summey North Charleston Library
9 a.m. - 5 p.m.
Phone: (843) 744-2489
John's Island Library
9 a.m. - 5 p.m.
Phone: (843) 559-1945
Hurd/St. Andrews Library
9 a.m. - 5 p.m.
Phone: (843) 766-2546
Folly Beach Library
9 a.m. - 2 p.m.
*open the 2nd and 4th Saturday
*open the 2nd and 4th Saturday
Phone: (843) 588-2001
Edisto Island Library
9 a.m. - 1 p.m.
Phone: (843) 869-2355
Dorchester Road Library
9 a.m. - 5 p.m.
Phone: (843) 552-6466
John L. Dart Library
9 a.m. - 5 p.m.
Phone: (843) 722-7550
Baxter-Patrick James Island
9 a.m. - 5 p.m.
Phone: (843) 795-6679
Main Library
9 a.m. - 5 p.m.
Phone: (843) 805-6930
Bees Ferry West Ashley Library
9 a.m. - 5 p.m.
Phone: (843) 805-6892
Edgar Allan Poe/Sullivan's Island Library
Closed for renovations
Phone: (843) 883-3914
Mobile Library
Closed
Phone: (843) 805-6909
Today's Hours
West Ashley Library
9 a.m. - 5 p.m.
Phone: (843) 766-6635
Wando Mount Pleasant Library
9 a.m. - 5 p.m.
Phone: (843) 805-6888
Village Library
9 a.m. - 1 p.m.
Phone: (843) 884-9741
St. Paul's/Hollywood Library
9 a.m. - 5 p.m.
Phone: (843) 889-3300
Otranto Road Library
9 a.m. - 5 p.m.
Phone: (843) 572-4094
Mt. Pleasant Library
9 a.m. – 5 p.m.
Phone: (843) 849-6161
McClellanville Library
9 a.m. – 1 p.m.
Phone: (843) 887-3699
Keith Summey North Charleston Library
9 a.m. - 5 p.m.
Phone: (843) 744-2489
John's Island Library
9 a.m. - 5 p.m.
Phone: (843) 559-1945
Hurd/St. Andrews Library
9 a.m. - 5 p.m.
Phone: (843) 766-2546
Folly Beach Library
9 a.m. - 2 p.m.
*open the 2nd and 4th Saturday
*open the 2nd and 4th Saturday
Phone: (843) 588-2001
Edisto Island Library
9 a.m. - 1 p.m.
Phone: (843) 869-2355
Dorchester Road Library
9 a.m. - 5 p.m.
Phone: (843) 552-6466
John L. Dart Library
9 a.m. - 5 p.m.
Phone: (843) 722-7550
Baxter-Patrick James Island
9 a.m. - 5 p.m.
Phone: (843) 795-6679
Main Library
9 a.m. - 5 p.m.
Phone: (843) 805-6930
Bees Ferry West Ashley Library
9 a.m. - 5 p.m.
Phone: (843) 805-6892
Edgar Allan Poe/Sullivan's Island Library
Closed for renovations
Phone: (843) 883-3914
Mobile Library
Closed
Phone: (843) 805-6909
Patron Login
menu
Item request has been placed!
×
Item request cannot be made.
×
Processing Request
Structure and stability of protein H and the M1 protein from Streptococcus pyogenes. Implications for other surface proteins of gram-positive bacteria.
Item request has been placed!
×
Item request cannot be made.
×
Processing Request
- Author(s): Nilson BH;Nilson BH; Frick IM; Akesson P; Forsén S; Björck L; Akerström B; Wikström M
- Source:
Biochemistry [Biochemistry] 1995 Oct 17; Vol. 34 (41), pp. 13688-98.- Publication Type:
Comparative Study; Journal Article; Research Support, Non-U.S. Gov't- Language:
English - Source:
- Additional Information
- Source: Publisher: American Chemical Society Country of Publication: United States NLM ID: 0370623 Publication Model: Print Cited Medium: Print ISSN: 0006-2960 (Print) Linking ISSN: 00062960 NLM ISO Abbreviation: Biochemistry Subsets: MEDLINE
- Publication Information: Original Publication: Washington, American Chemical Society.
- Subject Terms: Antigens, Bacterial* ; Bacterial Proteins* ; Gram-Positive Bacteria* ; Protein Structure, Secondary* ; Streptococcus pyogenes*; Bacterial Outer Membrane Proteins/*chemistry ; Carrier Proteins/*chemistry ; Membrane Proteins/*chemistry; Amino Acid Sequence ; Circular Dichroism ; Fourier Analysis ; Molecular Sequence Data ; Protein Denaturation ; Protein Folding ; Thermodynamics ; Urea
- Abstract: M proteins and other members of the M protein family, expressed on the surface of Streptococcus pyogenes, bind host proteins such as immunoglobulins, albumin, and fibrinogen. Protein H and the M1 protein are expressed by adjacent genes and both belong to the M protein family. In this work, the structure and stability of these two proteins have been investigated. As judged from sequence analysis and circular dichroism spectroscopy, the proteins are almost entirely in an alpha-helix conformation. The amino acids are arranged in a seven-residue (heptad) repeat pattern along the greater part of the proteins. These observations support the previously accepted model of M proteins as coiled-coil dimers. However, it was also found that the structures of both proteins were thermally unstable; i.e., the content of helix conformation was greatly reduced at 37 degrees C as compared to 25 degrees C or below. Together with previous findings that these proteins appear as monomers at 37 degrees C and dimers at low temperatures, the results suggest that the coiled-coil dimers are unfolded at 37 degrees C. The heptad patterns of protein H and the M1 protein showed a nonoptimal distribution of residues expected for a coiled-coil conformation. This is a possible explanation for the low thermal stability of the proteins. It was also demonstrated that the proteins were stabilized in the presence of the ligands IgG and/or albumin. Protein H and M1 protein show a high degree of sequence similarity in their C-terminal regions, and a fragment from this region displayed a high content of helix conformation, whereas fragments from the nonsimilar N-terminal parts did not adopt any stable folded structure. Thus, the C-terminal parts, which are conserved within the M protein family, may constitute a framework for the formation of the parallel helical coiled-coil structure, and we propose that the less stable N-terminal part may also participate in antiparallel interaction with M proteins on adjacent bacteria. The results suggest that temperature fluctuations in the environment could change the properties of bacterial surface proteins, thereby affecting the molecular interactions between the bacterium and its host.
- Accession Number: 0 (Antigens, Bacterial)
0 (Bacterial Outer Membrane Proteins)
0 (Bacterial Proteins)
0 (Carrier Proteins)
0 (Membrane Proteins)
0 (protein H, Streptococcus)
0 (streptococcal M protein)
8W8T17847W (Urea) - Publication Date: Date Created: 19951017 Date Completed: 19951214 Latest Revision: 20190613
- Publication Date: 20240829
- Accession Number: 10.1021/bi00041a051
- Accession Number: 7577960
- Source:
Contact CCPL
Copyright 2022 Charleston County Public Library Powered By EBSCO Stacks 3.3.0 [350.3] | Staff Login
No Comments.