Martinez-Fleites, Carlos, Smith, Nicola L., Turkenburg, Johan P. et al, 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
Full content URL: http://dx.doi.org/10.1107/S1744309109032813
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| Item Type: | Article |
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| Item Status: | Live Archive |
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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.
| 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. |
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| Keywords: | Hylp, phage tail, hyaluronate lyase |
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| Subjects: | C Biological Sciences > C700 Molecular Biology, Biophysics and Biochemistry |
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| Divisions: | College of Science > School of Life Sciences |
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| ID Code: | 6143 |
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| Deposited On: | 17 Sep 2012 10:35 |
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