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Structure paper

TitleThe function of hydrophobic residues in the catalytic cleft of Streptococcus pneumoniae hyaluronate lyase. Kinetic characterization of mutant enzyme forms
Journal, issue, pagesJ. Biol. Chem., Vol. 278, Page 3079-3088, Year 2003
Publish dateNov 16, 2002 (structure data deposition date)
AuthorsNukui, M. / Taylor, K.B. / McPherson, D.T. / Shigenaga, M. / Jedrzejas, M.J.
External linksJ. Biol. Chem. / PubMed:12446724
MethodsX-ray diffraction
Resolution1.5 - 2.3 Å
Structure data

PDB-1n7n:
Streptococcus pneumoniae Hyaluronate Lyase W292A Mutant
Method: X-RAY DIFFRACTION / Resolution: 1.55 Å

PDB-1n7o:
Streptococcus pneumoniae Hyaluronate Lyase F343V Mutant
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

PDB-1n7p:
Streptococcus pneumoniae Hyaluronate Lyase W292A/F343V Double Mutant
Method: X-RAY DIFFRACTION / Resolution: 1.55 Å

PDB-1n7q:
Streptococcus pneumoniae Hyaluronate Lyase W291A/W292A Double Mutant complex with hyaluronan hexasacchride
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-1n7r:
Streptococcus pneumoniae Hyaluronate Lyase W291A/W292A/F343V Mutant complex with hexasaccharide hyaluronan
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • streptococcus pneumoniae (bacteria)
KeywordsLYASE / protein mutant

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