1ojo
From Proteopedia
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SPECIFICITY AND MECHANISM OF STREPTOCOCCUS PNEUMONIAE HYALURONATE LYASE: COMPLEX OF THE TYR408PHE MUTANT WITH 4-SULPHATED CHONDROITIN DISACCHARIDE
Overview
Streptococcus pneumoniae hyaluronate lyase is a surface enzyme of this, Gram-positive bacterium. The enzyme degrades hyaluronan and, chondroitin/chondroitin sulfates by cleaving the beta1,4-glycosidic, linkage between the glycan units of these polymeric substrates. This, degradation helps spreading of this bacterial organism throughout the host, tissues and facilitates the disease process caused by pneumococci. The, mechanism of this degradative process is based on beta-elimination, is, termed proton acceptance and donation, and involves selected residues of a, well defined catalytic site of the enzyme. The degradation of hyaluronan, alone is thought to proceed through a processive mode of action. The, structures of complexes between the enzyme and chondroitin as well as, chondroitin ... [(full description)]
About this Structure
1OJO is a [Single protein] structure of sequence from [Streptococcus pneumoniae] with SO4 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
Structures of Streptococcus pneumoniae hyaluronate lyase in complex with chondroitin and chondroitin sulfate disaccharides. Insights into specificity and mechanism of action., Rigden DJ, Jedrzejas MJ, J Biol Chem. 2003 Dec 12;278(50):50596-606. Epub 2003 Sep 30. PMID:14523022
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