PDBsum entry: 2wh7

Hydrolase

PDB id: 2wh7

Contents

Protein chain

152 a.a. *

Waters ×200

* Residue conservation analysis

PDB id:

2wh7

Name:

Hydrolase

Title:

The partial structure of a group a streptpcoccal phage- encoded tail fibre hyaluronate lyase hylp2

Structure:

Hyaluronidase-phage associated. Chain: a. Fragment: hyaluronate lyases fragment, residues 215-372. Synonym: hylp2. Engineered: yes

Source:

Streptococcus pyogenes. Organism_taxid: 1314. Strain: m1 gas sf370. Atcc: 700294. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

1.60Å R-factor: 0.214 R-free: 0.258

Authors:

C.Martinez-Fleites,G.W.Black,J.P.Turkenburg,N.L.Smith, E.J.Taylor

Key ref:

C.Martinez-Fleites et al. (2009). Structures of two truncated phage-tail hyaluronate lyases from Streptococcus pyogenes serotype M1. Acta Crystallogr Sect F Struct Biol Cryst Commun, 65, 963-966. PubMed id: 19850999

Date:

01-May-09 Release date: 01-Sep-09

Protein chain

Q99ZZ7  (Q99ZZ7_STRP1) -  Hyaluronidase-phage associated

Seq: 372 a.a.

Struc: 152 a.a.

Enzyme reactions

• Enzyme class: E.C.3.2.1.35 - Hyaluronoglucosaminidase.
• Reaction: Random hydrolysis of 1->4-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate.

 Gene Ontology (GO) functional annotation 

• Biological process: capsule polysaccharide biosynthetic process (1 term)
• Biochemical function: hyalurononglucosaminidase activity (1 term)

Acta Crystallogr Sect F Struct Biol Cryst Commun 65:963-966 (2009)

PubMed id: 19850999

Structures of two truncated phage-tail hyaluronate lyases from Streptococcus pyogenes serotype M1.

C.Martinez-Fleites, N.L.Smith, J.P.Turkenburg, G.W.Black, E.J.Taylor.

ABSTRACT

The crystal structures of truncated forms of the Streptococcus pyogenes phage-encoded hyaluronate lyases HylP2 and HylP3 were determined by molecular replacement to 1.6 and 1.9 A resolution, respectively. The truncated forms crystallized in a hexagonal space group, forming a trimer around the threefold crystallographic axis. The arrangement of the fold is very similar to that observed in the structure of the related hyaluronate lyase HylP1. The structural elements putatively involved in substrate recognition are found to be conserved in both the HylP2 and HylP3 fragments.