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2WH7

The partial structure of a group A streptpcoccal phage-encoded tail fibre hyaluronate lyase Hylp2

Summary for 2WH7
Entry DOI10.2210/pdb2wh7/pdb
DescriptorHYALURONIDASE-PHAGE ASSOCIATED (2 entities in total)
Functional Keywordstriple-stranded beta-helix, hyaluronan lyase, phage tail fibre, hydrolase, glycosidase, hyaluronidase, scarlet fever
Biological sourceSTREPTOCOCCUS PYOGENES
Total number of polymer chains1
Total formula weight19118.58
Authors
Martinez-Fleites, C.,Black, G.W.,Turkenburg, J.P.,Smith, N.L.,Taylor, E.J. (deposition date: 2009-05-01, release date: 2009-09-01, Last modification date: 2023-12-13)
Primary citationMartinez-Fleites, C.,Smith, N.L.,Turkenburg, J.P.,Black, G.W.,Taylor, E.J.
Structures of Two Truncated Phage-Tail Hyaluronate Lyases from Streptococcus Pyogenes Serotype M1.
Acta Crystallogr.,Sect.F, 65:963-, 2009
Cited by
PubMed 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.
PubMed: 19850999
DOI: 10.1107/S1744309109032813
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.6 Å)
Structure validation

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