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InterPro: IPR011050 Pectin lyase fold/virulence factor

Protein matchesHelp
UniProtKB
Matches:
11341 proteins
AccessionHelp IPR011050 Pectin_lyase_fold/virulence
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Children IPR003992 Pertactin virulence factor, N-terminal
IPR012332 Phage P22 tailspike
IPR012334 Pectin lyase fold
Found in IPR000710 Peptidase S6, IgA endopeptidase
IPR017318 Peptidase S8A, subtilisin-related, campylobacter
Contains IPR004899 Pertactin
IPR006626 Parallel beta-helix repeat
IPR006633 Carbohydrate-binding/sugar hydrolysis domain
IPR007742 Periplasmic copper-binding
IPR008638 Filamentous haemagglutinin, N-terminal, bacterial
IPR011459 Protein of unknown function DUF1565
IPR013425 Autotransporter-associated beta strand repeat
IPR013687 Disaggregatase related-2
IPR018040 Pectinesterase, active site
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

Microbial pectin and pectate lyases are virulence factors that degrade the pectic components of the plant cell wall [1]. When the backbone of pectin is methylated it is known as pectin and is cleaved by pectin lyase, and when it is demethylated it is known as pectate and is cleaved by pectate lyase. Pectin lyase from Aspergillus niger displays a single-stranded, right-handed parallel beta-helix topology (IPR006626), where each coil contains three beta-strands and three turn regions. Several other virulence factors share this beta-helix topology, although they vary in the number of coils, including bacterial pectate lyases, fungal and bacterial galacturonases (such as rhamnogalacturonase and polygalacturonase), chrondroitinase B from Flavobacterium sp., iota-carrageenase from Alteromonas sp., pectin methylesterase (PemA), P22 tailspike protein from Enterobacteria phage P22, and the virulence factor P.69 pertactin from Bordetella pertussis that mediates adhesion to target mammalian cells [2].

Structural linksHelp
PDB - click here

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR011050 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O04953 Putative pectinesterase 52

O32591 Serine protease espP

P47180 Polygalacturonase

Q3TTP0 Uncharacterized protein C1orf14 homolog

Q86WI1 Fibrocystin-L

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR005546 Autotransporter beta-domain
IPR018040 Pectinesterase, active site
IPR006315 Outer membrane autotransporter barrel
IPR006626 Parallel beta-helix repeat
IPR014756 Immunoglobulin E-set
IPR002909 Cell surface receptor IPT/TIG
IPR006633 Carbohydrate-binding/sugar hydrolysis domain
IPR009003 Serine/cysteine peptidase, trypsin-like
IPR012332 Phage P22 tailspike
IPR012334 Pectin lyase fold
IPR000710 Peptidase S6, IgA endopeptidase
IPR000070 Pectinesterase, catalytic
IPR000743 Glycoside hydrolase, family 28
IPR019316 G8 domain
IPR011050 Pectin lyase fold/virulence factor
IPR008972 Cupredoxin
PDB Chain
ModBase
SWISS-MODEL

PublicationsHelp
1. Mayans O, Scott M, Connerton I, Gravesen T, Benen J, Visser J, Pickersgill R, Jenkins J.
Two crystal structures of pectin lyase A from Aspergillus reveal a pH driven conformational change and striking divergence in the substrate-binding clefts of pectin and pectate lyases.
Structure 5 677-89 1997 [PubMed: 9195887]
http://dx.doi.org/10.1016/S0969-2126(97)00222-0
2. Jenkins J, Mayans O, Pickersgill R.
Structure and evolution of parallel beta-helix proteins.
J. Struct. Biol. 122 236-46 1998 [PubMed: 9724625]
http://dx.doi.org/10.1006/jsbi.1998.3985

Additional ReadingHelp
Xiao Z, Bergeron H, Grosse S, Beauchemin M, Garron ML, Shaya D, Sulea T, Cygler M, Lau PC.
Improvement of the thermostability and activity of a pectate lyase by single amino acid substitutions, using a strategy based on melting-temperature-guided sequence alignment.
Appl. Environ. Microbiol. 74 2008 1183-9 [PubMed: 18156340]
http://dx.doi.org/10.1128/AEM.02220-07
Di Matteo A, Giovane A, Raiola A, Camardella L, Bonivento D, De Lorenzo G, Cervone F, Bellincampi D, Tsernoglou D.
Structural basis for the interaction between pectin methylesterase and a specific inhibitor protein.
Plant Cell 17 2005 849-58 [PubMed: 15722470]
http://dx.doi.org/10.1105/tpc.104.028886
Mizuno M, Koide A, Yamamura A, Akeboshi H, Yoshida H, Kamitori S, Sakano Y, Nishikawa A, Tonozuka T.
Crystal structure of Aspergillus niger isopullulanase, a member of glycoside hydrolase family 49.
J. Mol. Biol. 376 2008 210-20 [PubMed: 18155243]
http://dx.doi.org/10.1016/j.jmb.2007.11.098
Fries M, Ihrig J, Brocklehurst K, Shevchik VE, Pickersgill RW.
Molecular basis of the activity of the phytopathogen pectin methylesterase.
EMBO J. 26 2007 3879-87 [PubMed: 17717531]
http://dx.doi.org/10.1038/sj.emboj.7601816
Bonivento D, Pontiggia D, Matteo AD, Fernandez-Recio J, Salvi G, Tsernoglou D, Cervone F, Lorenzo GD, Federici L.
Crystal structure of the endopolygalacturonase from the phytopathogenic fungus Colletotrichum lupini and its interaction with polygalacturonase-inhibiting proteins.
Proteins 70 2008 294-9 [PubMed: 17876815]
http://dx.doi.org/10.1002/prot.21610
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InterPro 23.1