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InterPro: IPR018452 Cellulosome anchoring protein, cohesin domain, subgroup

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79 proteins

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Accession

IPR018452 Cohesin_dom_subgr

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:2.60.40.680	Cohesin	79
Signatures in BioMart

InterPro Relationships Help

Parent

IPR002102 Cellulosome anchoring protein, cohesin domain

GO Term annotation Help

Process

GO:0000272 polysaccharide catabolic process

Function

GO:0030246 carbohydrate binding

Component

GO:0009274 peptidoglycan-based cell wall

InterPro annotation

Entry Details in BioMart

Abstract

Cohesin domains interact with a complementary domain, termed the dockerin domain (see IPR002105). The cohesin-dockerin interaction is the crucial interaction for complex formation in the cellulosome [1].

The scaffoldin component of the cellulolytic bacterium Clostridium thermocellum is a non-hydrolytic protein which organises the hydrolytic enzymes in a large complex, called the cellulosome. Scaffoldin comprises a series of functional domains, amongst which is a single cellulose-binding domain and nine cohesin domains which are responsible for integrating the individual enzymatic subunits into the complex.

Structural links Help

PDB - click here

SCOP: b.2.2.2

CATH: 2.60.40.680

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR018452

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

Q06851 Cellulosomal-scaffolding protein A

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR008965	Carbohydrate-binding
IPR018452	Cellulosome anchoring protein, cohesin domain, subgroup
IPR016134	Cellulosome enzyme, dockerin type I
IPR018247	EF-Hand 1, calcium-binding site
IPR002105	Cellulosome enzyme, dockerin type I, calcium-binding motif
IPR002102	Cellulosome anchoring protein, cohesin domain
IPR001956	Bacterial type 3a, cellulose-binding
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Shimon LJ, Bayer EA, Morag E, Lamed R, Yaron S, Shoham Y, Frolow F. A cohesin domain from Clostridium thermocellum: the crystal structure provides new insights into cellulosome assembly. Structure 5 381-90 1997 [PubMed: 9083107] http://dx.doi.org/10.1016/S0969-2126(97)00195-0

Additional Reading Open in usermanual
	Carvalho AL, Dias FM, Nagy T, Prates JA, Proctor MR, Smith N, Bayer EA, Davies GJ, Ferreira LM, Romao MJ, Fontes CM, Gilbert HJ. Evidence for a dual binding mode of dockerin modules to cohesins. Proc. Natl. Acad. Sci. U.S.A. 104 2007 3089-94 [PubMed: 17360613] http://dx.doi.org/10.1073/pnas.0611173104
	Adams JJ, Pal G, Jia Z, Smith SP. Mechanism of bacterial cell-surface attachment revealed by the structure of cellulosomal type II cohesin-dockerin complex. Proc. Natl. Acad. Sci. U.S.A. 103 2006 305-10 [PubMed: 16384918] http://dx.doi.org/10.1073/pnas.0507109103
	Noach I, Frolow F, Jakoby H, Rosenheck S, Shimon LW, Lamed R, Bayer EA. Crystal structure of a type-II cohesin module from the Bacteroides cellulosolvens cellulosome reveals novel and distinctive secondary structural elements. J. Mol. Biol. 348 2005 1-12 [PubMed: 15808849] http://dx.doi.org/10.1016/j.jmb.2005.02.024
	Noach I, Frolow F, Alber O, Lamed R, Shimon LJ, Bayer EA. Intermodular linker flexibility revealed from crystal structures of adjacent cellulosomal cohesins of Acetivibrio cellulolyticus. J. Mol. Biol. 391 2009 86-97 [PubMed: 19501595]
	Pinheiro BA, Proctor MR, Martinez-Fleites C, Prates JA, Money VA, Davies GJ, Bayer EA, Fontesm CM, Fierobe HP, Gilbert HJ. The Clostridium cellulolyticum dockerin displays a dual binding mode for its cohesin partner. J. Biol. Chem. 283 2008 18422-30 [PubMed: 18445585] http://dx.doi.org/10.1074/jbc.M801533200

InterPro 23.1