2c3f
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Streptococcus pyogenes (group A Streptococcus) causes severe invasive | + | Streptococcus pyogenes (group A Streptococcus) causes severe invasive infections including scarlet fever, pharyngitis (streptococcal sore throat), skin infections, necrotizing fasciitis (flesh-eating disease), septicemia, erysipelas, cellulitis, acute rheumatic fever, and toxic shock. The conversion from nonpathogenic to toxigenic strains of S. pyogenes is frequently mediated by bacteriophage infection. One of the key bacteriophage-encoded virulence factors is a putative "hyaluronidase," HylP1, a phage tail-fiber protein responsible for the digestion of the S. pyogenes hyaluronan capsule during phage infection. Here we demonstrate that HylP1 is a hyaluronate lyase. The 3D structure, at 1.8-angstroms resolution, reveals an unusual triple-stranded beta-helical structure and provides insight into the structural basis for phage tail assembly and the role of phage tail proteins in virulence. Unlike the triple-stranded beta-helix assemblies of the bacteriophage T4 injection machinery and the tailspike endosialidase of the Escherichia coli K1 bacteriophage K1F, HylP1 possesses three copies of the active center on the triple-helical fiber itself without the need for an accessory catalytic domain. The triple-stranded beta-helix is not simply a structural scaffold, as previously envisaged; it is harnessed to provide a 200-angstroms-long substrate-binding groove for the optimal reduction in hyaluronan viscosity to aid phage penetration of the capsule. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptococcus pyogenes]] | [[Category: Streptococcus pyogenes]] | ||
| - | [[Category: Black, G | + | [[Category: Black, G W.]] |
| - | [[Category: Charnock, S | + | [[Category: Charnock, S J.]] |
| - | [[Category: Davies, G | + | [[Category: Davies, G J.]] |
| - | [[Category: Dodson, E | + | [[Category: Dodson, E J.]] |
[[Category: Linsay, A.]] | [[Category: Linsay, A.]] | ||
| - | [[Category: Smith, N | + | [[Category: Smith, N L.]] |
| - | [[Category: Taylor, E | + | [[Category: Taylor, E J.]] |
| - | [[Category: Turkenburg, J | + | [[Category: Turkenburg, J P.]] |
[[Category: NA]] | [[Category: NA]] | ||
[[Category: hyaluronan lyase]] | [[Category: hyaluronan lyase]] | ||
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[[Category: triple-stranded beta-helix]] | [[Category: triple-stranded beta-helix]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:44:27 2008'' |
Revision as of 14:44, 21 February 2008
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THE STRUCTURE OF A GROUP A STREPTOCOCCAL PHAGE-ENCODED TAIL-FIBRE SHOWING HYALURONAN LYASE ACTIVITY.
Overview
Streptococcus pyogenes (group A Streptococcus) causes severe invasive infections including scarlet fever, pharyngitis (streptococcal sore throat), skin infections, necrotizing fasciitis (flesh-eating disease), septicemia, erysipelas, cellulitis, acute rheumatic fever, and toxic shock. The conversion from nonpathogenic to toxigenic strains of S. pyogenes is frequently mediated by bacteriophage infection. One of the key bacteriophage-encoded virulence factors is a putative "hyaluronidase," HylP1, a phage tail-fiber protein responsible for the digestion of the S. pyogenes hyaluronan capsule during phage infection. Here we demonstrate that HylP1 is a hyaluronate lyase. The 3D structure, at 1.8-angstroms resolution, reveals an unusual triple-stranded beta-helical structure and provides insight into the structural basis for phage tail assembly and the role of phage tail proteins in virulence. Unlike the triple-stranded beta-helix assemblies of the bacteriophage T4 injection machinery and the tailspike endosialidase of the Escherichia coli K1 bacteriophage K1F, HylP1 possesses three copies of the active center on the triple-helical fiber itself without the need for an accessory catalytic domain. The triple-stranded beta-helix is not simply a structural scaffold, as previously envisaged; it is harnessed to provide a 200-angstroms-long substrate-binding groove for the optimal reduction in hyaluronan viscosity to aid phage penetration of the capsule.
About this Structure
2C3F is a Single protein structure of sequence from Streptococcus pyogenes with as ligand. Active as Hyaluronate lyase, with EC number 4.2.2.1 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Structure of a group A streptococcal phage-encoded virulence factor reveals a catalytically active triple-stranded beta-helix., Smith NL, Taylor EJ, Lindsay AM, Charnock SJ, Turkenburg JP, Dodson EJ, Davies GJ, Black GW, Proc Natl Acad Sci U S A. 2005 Dec 6;102(49):17652-7. Epub 2005 Nov 28. PMID:16314578
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