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

Martinez-Fleites, Carlos and Smith, Nicola L. and Turkenburg, Johan P. and Black, Gary W. and Taylor, Edward (2009) Structures of two truncated phage-tail hyaluronate lyases from Streptococcus pyogenes serotype M1. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 65 (10). pp. 963-966. ISSN 1744-3091

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Full text URL: http://dx.doi.org/10.1107/S1744309109032813

Abstract

he crystal structures of truncated forms of the Streptococcus pyogenes phageencoded 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.

Item Type:Article
Additional Information:he crystal structures of truncated forms of the Streptococcus pyogenes phageencoded 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.
Keywords:Hylp, phage tail, hyaluronate lyase
Subjects:C Biological Sciences > C700 Molecular Biology, Biophysics and Biochemistry
Divisions:College of Science > School of Life Sciences
ID Code:6143
Deposited By: Edward Taylor
Deposited On:17 Sep 2012 10:35
Last Modified:13 Mar 2013 09:13

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