From Proteopedia
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| - | [[Image:2o0i.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:2o0i.png|left|200px]] |
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| | {{STRUCTURE_2o0i| PDB=2o0i | SCENE= }} | | {{STRUCTURE_2o0i| PDB=2o0i | SCENE= }} |
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| - | '''crystal structure of the R185A mutant of the N-terminal domain of the Group B Streptococcus Alpha C protein'''
| + | ===crystal structure of the R185A mutant of the N-terminal domain of the Group B Streptococcus Alpha C protein=== |
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| - | ==Overview==
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| - | Group B Streptococcus (GBS) frequently colonizes the human gastrointestinal and gynecological tracts and less frequently causes deep tissue infections. The transition between colonization and infection depends upon the ability of the organism to cross epithelial barriers. The alpha C protein (ACP) on the surface of GBS contributes to this process. A virulence factor in mouse models of infection, and prototype for a family of Gram-positive bacterial surface proteins, ACP facilitates GBS entry into human cervical epithelial cells and movement across cell layers. ACP binds to host cell surface glycosaminoglycan (GAG). From crystallography, we have identified a cluster of basic residues (BR2) that is a putative GAG binding area in Domain 2, near the junction of the N-terminal domain of ACP and the first of a series of tandem amino acid repeats. D2-R, a protein construct including this region, binds to cells similarly to full-length ACP. We now demonstrate that the predicted charged BR2 residues confer GAG binding; site-directed mutagenesis of these residues (Arg(172), Arg(185), or Lys(196)) eliminates cell-binding activity of construct D2-R. In addition, we have constructed a GBS strain expressing a variant ACP with a charge-neutralizing substitution at residue 185. This strain enters host cells less effectively than does the wild-type strain and similarly to an ACP null mutant strain. The point mutant strain transcytoses similarly to the wild-type strain. These data indicate that GAG-binding activity underlies ACP-mediated cellular entry of GBS. GBS entry into host cells and transcytosis of host cells may occur by distinct mechanisms.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_17259175}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17259175 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_17259175}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Fibronectin fold]] | | [[Category: Fibronectin fold]] |
| | [[Category: Surface active protein]] | | [[Category: Surface active protein]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 10:09:12 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:42:55 2008'' |
Revision as of 10:42, 29 July 2008
Template:STRUCTURE 2o0i
crystal structure of the R185A mutant of the N-terminal domain of the Group B Streptococcus Alpha C protein
Template:ABSTRACT PUBMED 17259175
About this Structure
2O0I is a Single protein structure of sequence from Streptococcus agalactiae serogroup ia. Full crystallographic information is available from OCA.
Reference
Identification of a glycosaminoglycan binding region of the alpha C protein that mediates entry of group B Streptococci into host cells., Baron MJ, Filman DJ, Prophete GA, Hogle JM, Madoff LC, J Biol Chem. 2007 Apr;282(14):10526-36. Epub 2007 Jan 26. PMID:17259175
Page seeded by OCA on Tue Jul 29 13:42:55 2008
