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3h73
From Proteopedia
Revision as of 13:03, 29 September 2014 by OCA (Talk | contribs)
3h73 is a 2 chain structure with sequence from Streptococcus pneumoniae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Currently there is pressing need to develop novel therapeutic agents for the treatment of infections by the human respiratory pathogens Pseudomonas aeruginosa and Streptococcus pneumoniae. The neuraminidases of these pathogens are important for host colonization in animal models of infection and are attractive targets for drug discovery. To aid in the development of inhibitors against these neuraminidases, we have determined the crystal structures of the P. aeruginosa enzyme NanPs and S. pneumoniae enzyme NanA at 1.6 and 1.7A resolution, respectively. In situ proteolysis with trypsin was essential for the crystallization of our recombinant NanA. The active site regions of the two enzymes are strikingly different. NanA contains a deep pocket that is similar to that in canonical neuraminidases, while the NanPs active site is much more open. The comparative studies suggest that NanPs may not be a classical neuraminidase, and may have distinct natural substrates and physiological functions. This work represents an important step in the development of drugs to prevent respiratory tract colonization by these two pathogens.
Crystal structures of respiratory pathogen neuraminidases.,Hsiao YS, Parker D, Ratner AJ, Prince A, Tong L Biochem Biophys Res Commun. 2009 Mar 13;380(3):467-71. Epub 2009 Jan 23. PMID:19284989[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Hsiao YS, Parker D, Ratner AJ, Prince A, Tong L. Crystal structures of respiratory pathogen neuraminidases. Biochem Biophys Res Commun. 2009 Mar 13;380(3):467-71. Epub 2009 Jan 23. PMID:19284989 doi:http://dx.doi.org/10.1016/j.bbrc.2009.01.108
