2c3f

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2c3f.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2c3f.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2c3f| PDB=2c3f | SCENE= }}
{{STRUCTURE_2c3f| PDB=2c3f | SCENE= }}
-
'''THE STRUCTURE OF A GROUP A STREPTOCOCCAL PHAGE-ENCODED TAIL-FIBRE SHOWING HYALURONAN LYASE ACTIVITY.'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16314578}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16314578 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16314578}}
==About this Structure==
==About this Structure==
Line 36: Line 40:
[[Category: Scarlet fever]]
[[Category: Scarlet fever]]
[[Category: Triple-stranded beta-helix]]
[[Category: Triple-stranded beta-helix]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 21:11:22 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 22:21:54 2008''

Revision as of 19:21, 27 July 2008

Template:STRUCTURE 2c3f

THE STRUCTURE OF A GROUP A STREPTOCOCCAL PHAGE-ENCODED TAIL-FIBRE SHOWING HYALURONAN LYASE ACTIVITY.

Template:ABSTRACT PUBMED 16314578

About this Structure

2C3F is a Single protein structure of sequence from Streptococcus pyogenes. 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

Page seeded by OCA on Sun Jul 27 22:21:54 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools