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2pz4

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[[Image:2pz4.jpg|left|200px]]<br /><applet load="2pz4" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2pz4.jpg|left|200px]]
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caption="2pz4, resolution 1.800&Aring;" />
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'''Crystal Structure of SpaB (GBS52), the minor pilin in gram-positive pathogen Streptococcus agalactiae'''<br />
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{{Structure
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|PDB= 2pz4 |SIZE=350|CAPTION= <scene name='initialview01'>2pz4</scene>, resolution 1.800&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY=
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'''Crystal Structure of SpaB (GBS52), the minor pilin in gram-positive pathogen Streptococcus agalactiae'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2PZ4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_agalactiae Streptococcus agalactiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PZ4 OCA].
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2PZ4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_agalactiae Streptococcus agalactiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PZ4 OCA].
==Reference==
==Reference==
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An IgG-like domain in the minor pilin GBS52 of Streptococcus agalactiae mediates lung epithelial cell adhesion., Krishnan V, Gaspar AH, Ye N, Mandlik A, Ton-That H, Narayana SV, Structure. 2007 Aug;15(8):893-903. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17697995 17697995]
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An IgG-like domain in the minor pilin GBS52 of Streptococcus agalactiae mediates lung epithelial cell adhesion., Krishnan V, Gaspar AH, Ye N, Mandlik A, Ton-That H, Narayana SV, Structure. 2007 Aug;15(8):893-903. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17697995 17697995]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Streptococcus agalactiae]]
[[Category: Streptococcus agalactiae]]
[[Category: Krishnan, V.]]
[[Category: Krishnan, V.]]
[[Category: Narayana, S.]]
[[Category: Narayana, S.]]
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[[Category: adhesions]]
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[[Category: adhesion]]
[[Category: cell adhesion]]
[[Category: cell adhesion]]
[[Category: gbs52]]
[[Category: gbs52]]
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[[Category: gram-positive pilins]]
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[[Category: gram-positive pilin]]
[[Category: igg-like domain]]
[[Category: igg-like domain]]
[[Category: spab]]
[[Category: spab]]
[[Category: streptococcus agalactiae]]
[[Category: streptococcus agalactiae]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:34:23 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:19:45 2008''

Revision as of 16:19, 20 March 2008


PDB ID 2pz4

Drag the structure with the mouse to rotate
, resolution 1.800Å
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of SpaB (GBS52), the minor pilin in gram-positive pathogen Streptococcus agalactiae


Overview

Streptococcus agalactiae is the leading cause of neonatal pneumonia, sepsis, and meningitis. The pathogen assembles heterotrimeric pilus structures on its surface; however, their function in pathogenesis is poorly understood. We report here the crystal structure of the pilin GBS52, which reveals two IgG-like fold domains, N1 and N2. Each domain is comprised of seven antiparallel beta strands, an arrangement similar to the fold observed in the Staphylococcus aureus adhesin Cna. Consistent with its role as an adhesin, deletion of gbs52 gene significantly reduces bacterial adherence to pulmonary epithelial cells. Moreover, latex beads linked to the GBS52 protein adhere to pulmonary but not to many other epithelial cells; binding to the former is specifically inhibited by antibodies against GBS52. Nonetheless, substantial binding is only observed with N2 domain-conjugated beads. This study presents the structure of a Gram-positive pilin that utilizes a distinct IgG fold variant to mediate pathogen adherence to a specific tissue.

About this Structure

2PZ4 is a Single protein structure of sequence from Streptococcus agalactiae. Full crystallographic information is available from OCA.

Reference

An IgG-like domain in the minor pilin GBS52 of Streptococcus agalactiae mediates lung epithelial cell adhesion., Krishnan V, Gaspar AH, Ye N, Mandlik A, Ton-That H, Narayana SV, Structure. 2007 Aug;15(8):893-903. PMID:17697995

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