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2brv
From Proteopedia
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CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE HYALURONATE LYASE FROM 70PERCENT SATURATED MALONATE.
Overview
Streptococcus pneumoniae hyaluronan lyase is a surface enzyme of this, Gram-positive bacterium. The enzyme degrades several biologically, important, information-rich linear polymeric glycans: hyaluronan, unsulfated chondroitin, and some chondroitin sulfates. This degradation, facilitates spreading of bacteria throughout the host tissues and, presumably provides energy and a carbon source for pneumococcal cells. Its, beta-elimination catalytic mechanism is an acid/base process termed proton, acceptance and donation leading to cleavage of beta-1,4 linkages of the, substrates. The degradation of hyaluronan occurs in two stages, initial, endolytic cuts are followed by processive exolytic cleavage of one, disaccharide at a time. In contrast, the degradation of chondroitins is, purely ... [(full description)]
About this Structure
2BRV is a [Single protein] structure of sequence from [Streptococcus pneumoniae] with MLA as [ligand]. Active as [Hyaluronate lyase], with EC number [4.2.2.1]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Alternate structural conformations of Streptococcus pneumoniae hyaluronan lyase: insights into enzyme flexibility and underlying molecular mechanism of action., Rigden DJ, Littlejohn JE, Joshi HV, de Groot BL, Jedrzejas MJ, J Mol Biol. 2006 May 12;358(4):1165-78. Epub 2006 Mar 13. PMID:16569416
Page seeded by OCA on Tue Oct 30 16:46:28 2007
