PDBsum entry 2yw0

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protein links
Lyase PDB id
Protein chain
332 a.a. *
Waters ×108
* Residue conservation analysis
PDB id:
Name: Lyase
Title: Crystal structure of hyluranidase trimer at 2.6 a resolution
Structure: Hyaluronidase, phage associated. Chain: a. Engineered: yes
Source: Streptococcus pyogenes serotype m1. Organism_taxid: 301447. Strain: serotype m1. Gene: hyl p2. Expressed in: escherichia coli. Expression_system_taxid: 562.
2.60Å     R-factor:   0.193     R-free:   0.219
Authors: R.Prem Kumar,P.Mishra,N.Singh,M.Perbandt,P.Kaur,S.Sharma,C.B V.Bhakuni,T.P.Singh
Key ref: P.Mishra et al. (2009). Polysaccharide binding sites in hyaluronate lyase--crystal structures of native phage-encoded hyaluronate lyase and its complexes with ascorbic acid and lactose. FEBS J, 276, 3392-3402. PubMed id: 19438710
18-Apr-07     Release date:   01-May-07    
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Protein chain
Pfam   ArchSchema ?
Q9A0M7  (Q9A0M7_STRP1) -  Hyaluronidase, phage associated
337 a.a.
332 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     capsule polysaccharide biosynthetic process   1 term 
  Biochemical function     hyalurononglucosaminidase activity     1 term  


FEBS J 276:3392-3402 (2009)
PubMed id: 19438710  
Polysaccharide binding sites in hyaluronate lyase--crystal structures of native phage-encoded hyaluronate lyase and its complexes with ascorbic acid and lactose.
P.Mishra, R.Prem Kumar, A.S.Ethayathulla, N.Singh, S.Sharma, M.Perbandt, C.Betzel, P.Kaur, A.Srinivasan, V.Bhakuni, T.P.Singh.
Hyaluronate lyases are a class of endoglycosaminidase enzymes with a high level of complexity and heterogeneity. The main function of the Streptococcus pyogenes bacteriophage protein hyaluronate lyase, HylP2, is to degrade hyaluronan into unsaturated disaccharide units. HylP2 was cloned, over-expressed and purified to homogeneity. The recombinant HylP2 exists as a homotrimer with a molecular mass of approximately 110 kDa under physiological conditions. The HylP2 was crystallized and the crystals were soaked in two separate reservoir solutions containing ascorbic acid and lactose, respectively. The crystal structures of native HylP2 and its two complexes with ascorbic acid and lactose have been determined. HylP2 folds into four distinct domains with a central core consisting of 16 antiparallel beta-strands forming an irregular triangular tube designated as triple-stranded beta-helix. The structures of complexes show that three molecules each of ascorbic acid and lactose bind to protein at the sugar binding groove in the triple-stranded beta-helix domain. Both ascorbic acid and lactose molecules occupy almost identical subsites in the long saccharide binding groove. Both ligands are involved in several hydrogen bonded interactions at each subsite. The binding characteristics and stereochemical properties indicate that Tyr264 may be involved in the catalytic activity of HylP2. The mutation of Tyr264 to Phe264 supports this observation.

Literature references that cite this PDB file's key reference

  PubMed id Reference
21330133 E.C.Schulz, and R.Ficner (2011).
Knitting and snipping: chaperones in β-helix folding.
  Curr Opin Struct Biol, 21, 232-239.  
21287626 Z.H.Elmabrouk, F.Vincent, M.Zhang, N.L.Smith, J.P.Turkenburg, S.J.Charnock, G.W.Black, and E.J.Taylor (2011).
Crystal structures of a family 8 polysaccharide lyase reveal open and highly occluded substrate-binding cleft conformations.
  Proteins, 79, 965-974.
PDB codes: 2wco 2wda 2x03
20805221 M.L.Garron, and M.Cygler (2010).
Structural and mechanistic classification of uronic acid-containing polysaccharide lyases.
  Glycobiology, 20, 1547-1573.  
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