2WH7
The partial structure of a group A streptpcoccal phage-encoded tail fibre hyaluronate lyase Hylp2
Summary for 2WH7
Entry DOI | 10.2210/pdb2wh7/pdb |
Descriptor | HYALURONIDASE-PHAGE ASSOCIATED (2 entities in total) |
Functional Keywords | triple-stranded beta-helix, hyaluronan lyase, phage tail fibre, hydrolase, glycosidase, hyaluronidase, scarlet fever |
Biological source | STREPTOCOCCUS PYOGENES |
Total number of polymer chains | 1 |
Total formula weight | 19118.58 |
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 citation | Martinez-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: 19850999DOI: 10.1107/S1744309109032813 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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