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1ywm

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{{STRUCTURE_1ywm| PDB=1ywm | SCENE= }}
{{STRUCTURE_1ywm| PDB=1ywm | SCENE= }}
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'''Crystal structure of the N-terminal domain of group B Streptococcus alpha C protein'''
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===Crystal structure of the N-terminal domain of group B Streptococcus alpha C protein===
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==Overview==
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Group B Streptococcus (GBS) is the leading cause of bacterial pneumonia, sepsis, and meningitis among neonates and an important cause of morbidity among pregnant women and immunocompromised adults. Invasive diseases due to GBS are attributed to the ability of the pathogen to translocate across human epithelial surfaces. The alpha C protein (ACP) has been identified as an invasin that plays a role in internalization and translocation of GBS across epithelial cells. The soluble N-terminal domain of ACP (NtACP) blocks the internalization of GBS. We determined the 1.86-A resolution crystal structure of NtACP comprising residues Ser(52) through Leu(225) of the full-length ACP. NtACP has two domains, an N-terminal beta-sandwich and a C-terminal three-helix bundle. Structural and topological alignments reveal that the beta-sandwich shares structural elements with the type III fibronectin fold (FnIII), but includes structural elaborations that make it unique. We have identified a potential integrin-binding motif consisting of Lys-Thr-Asp(146), Arg(110), and Asp(118). A similar arrangement of charged residues has been described in other invasins. ACP shows a heparin binding activity that requires NtACP. We propose a possible heparin-binding site, including one surface of the three-helix bundle, and nearby portions of the sandwich and repeat domains. We have validated this prediction using assays of the heparin binding and cell-adhesion properties of engineered fragments of ACP. This is the first crystal structure of a member of the highly conserved Gram-positive surface alpha-like protein family, and it will enable the internalization mechanism of GBS to be dissected at the atomic level.
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(as it appears on PubMed at http://www.pubmed.gov), where 15753100 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15753100}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Crystal structure of the N-terminal domain of the group B streptococcus alpha C protein., Auperin TC, Bolduc GR, Baron MJ, Heroux A, Filman DJ, Madoff LC, Hogle JM, J Biol Chem. 2005 May 6;280(18):18245-52. Epub 2005 Mar 6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15753100 15753100]
Crystal structure of the N-terminal domain of the group B streptococcus alpha C protein., Auperin TC, Bolduc GR, Baron MJ, Heroux A, Filman DJ, Madoff LC, Hogle JM, J Biol Chem. 2005 May 6;280(18):18245-52. Epub 2005 Mar 6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15753100 15753100]
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Large, identical, tandem repeating units in the C protein alpha antigen gene, bca, of group B streptococci., Michel JL, Madoff LC, Olson K, Kling DE, Kasper DL, Ausubel FM, Proc Natl Acad Sci U S A. 1992 Nov 1;89(21):10060-4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1438195 1438195]
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The alpha C protein mediates internalization of group B Streptococcus within human cervical epithelial cells., Bolduc GR, Baron MJ, Gravekamp C, Lachenauer CS, Madoff LC, Cell Microbiol. 2002 Nov;4(11):751-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12427097 12427097]
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Alpha C protein of group B Streptococcus binds host cell surface glycosaminoglycan and enters cells by an actin-dependent mechanism., Baron MJ, Bolduc GR, Goldberg MB, Auperin TC, Madoff LC, J Biol Chem. 2004 Jun 4;279(23):24714-23. Epub 2004 Mar 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15044471 15044471]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Streptococcus agalactiae]]
[[Category: Streptococcus agalactiae]]
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[[Category: Beta sandwich]]
[[Category: Beta sandwich]]
[[Category: Fibronectin fold]]
[[Category: Fibronectin fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:53:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:07:01 2008''

Revision as of 09:07, 29 July 2008

Image:1ywm.png

Template:STRUCTURE 1ywm

Crystal structure of the N-terminal domain of group B Streptococcus alpha C protein

Template:ABSTRACT PUBMED 15753100

About this Structure

1YWM is a Single protein structure of sequence from Streptococcus agalactiae. Full crystallographic information is available from OCA.

Reference

Crystal structure of the N-terminal domain of the group B streptococcus alpha C protein., Auperin TC, Bolduc GR, Baron MJ, Heroux A, Filman DJ, Madoff LC, Hogle JM, J Biol Chem. 2005 May 6;280(18):18245-52. Epub 2005 Mar 6. PMID:15753100

Large, identical, tandem repeating units in the C protein alpha antigen gene, bca, of group B streptococci., Michel JL, Madoff LC, Olson K, Kling DE, Kasper DL, Ausubel FM, Proc Natl Acad Sci U S A. 1992 Nov 1;89(21):10060-4. PMID:1438195

The alpha C protein mediates internalization of group B Streptococcus within human cervical epithelial cells., Bolduc GR, Baron MJ, Gravekamp C, Lachenauer CS, Madoff LC, Cell Microbiol. 2002 Nov;4(11):751-8. PMID:12427097

Alpha C protein of group B Streptococcus binds host cell surface glycosaminoglycan and enters cells by an actin-dependent mechanism., Baron MJ, Bolduc GR, Goldberg MB, Auperin TC, Madoff LC, J Biol Chem. 2004 Jun 4;279(23):24714-23. Epub 2004 Mar 23. PMID:15044471

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