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InterPro: IPR006626 Parallel beta-helix repeat

Protein matches Help

UniProtKB

Matches:

5951 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR006626 PbH1

Type

Repeat

Signatures Help

Database	ID	Name	Proteins
SMART	SM00710	PbH1	5951
Signatures in BioMart

InterPro Relationships Help

Found in

IPR000743 Glycoside hydrolase, family 28
IPR002022 Pectate lyase/Amb allergen
IPR006633 Carbohydrate-binding/sugar hydrolysis domain
IPR011050 Pectin lyase fold/virulence factor
IPR011459 Protein of unknown function DUF1565
IPR012334 Pectin lyase fold
IPR013687 Disaggregatase related-2
IPR015331 Bacteriophage P22, tailspike
IPR018082 AmbAllergen

InterPro annotation

Entry Details in BioMart

Abstract

The tertiary structures of pectate lyases and rhamnogalacturonase A show a stack of parallel beta strands that are coiled into a large helix. Each coil of the helix represents a structural repeat that, in some homologues, can be recognised from sequence information alone. Conservation of asparagines might be connected with asparagine-ladders that contribute to the stability of the fold. Proteins containing these repeats most often are enzymes with polysaccharide substrates [1].

Structural links Help

PDB - click here

SCOP: b.80.1.3 , b.80.1.6 , b.80.1.9

CATH: 2.160.20.10 , 2.160.20.20

Database links Help

Blocks: IPB006626

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR006626

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O22818 Probable polygalacturonase At2g43860

P0C1A6 Pectate lyase L

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
IPR006626	Parallel beta-helix repeat
IPR014756	Immunoglobulin E-set
IPR006633	Carbohydrate-binding/sugar hydrolysis domain
IPR002909	Cell surface receptor IPT/TIG
IPR012334	Pectin lyase fold
IPR000743	Glycoside hydrolase, family 28
IPR019316	G8 domain
IPR011050	Pectin lyase fold/virulence factor
IPR008972	Cupredoxin
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP Domain

Publications Open in usermanual
1.	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 Reading Open in usermanual
	Jenkins J, Shevchik VE, Hugouvieux-Cotte-Pattat N, Pickersgill RW. The crystal structure of pectate lyase Pel9A from Erwinia chrysanthemi. J. Biol. Chem. 279 2004 9139-45 [PubMed: 14670977] http://dx.doi.org/10.1074/jbc.M311390200
	van Pouderoyen G, Snijder HJ, Benen JA, Dijkstra BW. Structural insights into the processivity of endopolygalacturonase I from Aspergillus niger. FEBS Lett. 554 2003 462-6 [PubMed: 14623112] http://dx.doi.org/10.1016/S0014-5793(03)01221-3
	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
	Cho SW, Lee S, Shin W. The X-ray structure of Aspergillus aculeatus polygalacturonase and a modeled structure of the polygalacturonase-octagalacturonate complex. J. Mol. Biol. 311 2001 863-78 [PubMed: 11518536] http://dx.doi.org/10.1006/jmbi.2001.4919
	Shimizu T, Nakatsu T, Miyairi K, Okuno T, Kato H. Active-site architecture of endopolygalacturonase I from Stereum purpureum revealed by crystal structures in native and ligand-bound forms at atomic resolution. Biochemistry 41 2002 6651-9 [PubMed: 12022868] http://dx.doi.org/10.1021/bi025541a

InterPro 23.1