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InterPro: IPR004103 Polysaccharide lyase family 8, C-terminal

Protein matchesHelp
UniProtKB
Matches:
283 proteins
AccessionHelp IPR004103 Lyase_8_C
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR011071 Polysaccharide lyase family 8-like, C-terminal
GO Term annotationHelp
Function GO:0016829 lyase activity
Component GO:0005576 extracellular region
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

Proteins containing this domain consist of a group of secreted bacterial lyase enzymes capable of acting on hyaluronan (hyaluronate lyase, EC:4.2.2.1) and chondroitin (chondroitin AC lyase, EC:4.2.2.5) in the extracellular matrix of host tissues, contributing to the invasive capacity of the pathogen [1, 2]. This domain is almost always associated with the polysaccharide lyase family 8, N-terminal domain (see IPR003159). This entry represents the C-terminal domain of hyaluronate and chondroitin AC lyase enzymes.

Structural linksHelp
SCOP: b.24.1.1 , b.30.5.2
CATH: 2.60.220.10
Database linksHelp
Enzyme: EC:4.2.2
PANDIT: PF02884
Blocks: IPB004103

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR004103 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P59807 Chondroitin ABC endolyase 1

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR014718 Glycoside hydrolase-type carbohydrate-binding, subgroup
IPR012329 Polysaccharide lyase family 8, N-terminal
IPR004103 Polysaccharide lyase family 8, C-terminal
IPR011013 Glycoside hydrolase-type carbohydrate-binding
IPR008929 Chondroitin AC/alginate lyase
IPR011071 Polysaccharide lyase family 8-like, C-terminal
IPR015177 Lyase, catalytic
IPR008979 Galactose-binding domain-like
IPR015176 Lyase, N-terminal
IPR003159 Polysaccharide lyase family 8, central domain
PDB Chain
ModBase
CATH Domain
SCOP Domain

PublicationsHelp
1. Rigden DJ, Jedrzejas MJ.
Structures of Streptococcus pneumoniae hyaluronate lyase in complex with chondroitin and chondroitin sulfate disaccharides. Insights into specificity and mechanism of action.
J. Biol. Chem. 278 50596-606 2003 [PubMed: 14523022]
http://dx.doi.org/10.1074/jbc.M307596200
2. Fethiere J, Eggimann B, Cygler M.
Crystal structure of chondroitin AC lyase, a representative of a family of glycosaminoglycan degrading enzymes.
J. Mol. Biol. 288 635-47 1999 [PubMed: 10329169]
http://dx.doi.org/10.1006/jmbi.1999.2698

Additional ReadingHelp
Maruyama Y, Mikami B, Hashimoto W, Murata K.
A structural factor responsible for substrate recognition by Bacillus sp. GL1 xanthan lyase that acts specifically on pyruvated side chains of xanthan.
Biochemistry 46 2007 781-91 [PubMed: 17223699]
http://dx.doi.org/10.1021/bi0619775
Rigden DJ, Littlejohn JE, Joshi HV, de Groot BL, Jedrzejas MJ.
Alternate structural conformations of Streptococcus pneumoniae hyaluronan lyase: insights into enzyme flexibility and underlying molecular mechanism of action.
J. Mol. Biol. 358 2006 1165-78 [PubMed: 16569416]
http://dx.doi.org/10.1016/j.jmb.2006.02.066
Farrell AM, Taylor D, Holland KT.
Cloning, nucleotide sequence determination and expression of the Staphylococcus aureus hyaluronate lyase gene.
FEMS Microbiol. Lett. 130 1995 81-5 [PubMed: 7557301]
http://dx.doi.org/10.1016/0378-1097(95)00187-A
Lunin VV, Li Y, Linhardt RJ, Miyazono H, Kyogashima M, Kaneko T, Bell AW, Cygler M.
High-resolution crystal structure of Arthrobacter aurescens chondroitin AC lyase: an enzyme-substrate complex defines the catalytic mechanism.
J. Mol. Biol. 337 2004 367-86 [PubMed: 15003453]
http://dx.doi.org/10.1016/j.jmb.2003.12.071
Rigden DJ, Botzki A, Nukui M, Mewbourne RB, Lamani E, Braun S, von Angerer E, Bernhardt G, Dove S, Buschauer A, Jedrzejas MJ.
Design of new benzoxazole-2-thione-derived inhibitors of Streptococcus pneumoniae hyaluronan lyase: structure of a complex with a 2-phenylindole.
Glycobiology 16 2006 757-65 [PubMed: 16638841]
http://dx.doi.org/10.1093/glycob/cwj116
Maruyama Y, Hashimoto W, Mikami B, Murata K.
Crystal structure of Bacillus sp. GL1 xanthan lyase complexed with a substrate: insights into the enzyme reaction mechanism.
J. Mol. Biol. 350 2005 974-86 [PubMed: 15979090]
http://dx.doi.org/10.1016/j.jmb.2005.05.055
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InterPro 23.1