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

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.

SUBMITTER: Martinez-Fleites C

PROVIDER: S-EPMC2765878 | biostudies-literature | 2009 Oct

REPOSITORIES: biostudies-literature

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

Martinez-Fleites Carlos C Smith Nicola L NL Turkenburg Johan P JP Black Gary W GW Taylor Edward J EJ

Acta crystallographica. Section F, Structural biology and crystallization communications 20090918 Pt 10

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 substrat ...[more]

PMID: 19850999

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