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2b59

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Revision as of 05:04, 10 September 2015

The type II cohesin dockerin complex

Structural highlights

2b59 is a 2 chain structure with sequence from Atcc 27405 and Cloth. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	SdbA (CLOTH), cipA (ATCC 27405)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, TOPSAN

Function

[CIPA_CLOTH] Acts as a scaffolding protein in the cellulosome. It promotes binding of cellulose to the catalytic domains of the cellulolytic enzymes.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Bacterial cell-surface attachment of macromolecular complexes maintains the microorganism in close proximity to extracellular substrates and allows for optimal uptake of hydrolytic byproducts. The cellulosome is a large multienzyme complex used by many anaerobic bacteria for the efficient degradation of plant cell-wall polysaccharides. The mechanism of cellulosome retention to the bacterial cell surface involves a calcium-mediated protein-protein interaction between the dockerin (Doc) module from the cellulosomal scaffold and a cohesin (Coh) module of cell-surface proteins located within the proteoglycan layer. Here, we report the structure of an ultra-high-affinity (K(a) = 1.44 x 10(10) M(-1)) complex between type II Doc, together with its neighboring X module from the cellulosome scaffold of Clostridium thermocellum, and a type II Coh module associated with the bacterial cell surface. Identification of X module-Doc and X module-Coh contacts reveal roles for the X module in Doc stability and enhanced Coh recognition. This extremely tight interaction involves one face of the Coh and both helices of the Doc and comprises significant hydrophobic character and a complementary extensive hydrogen-bond network. This structure represents a unique mechanism for cell-surface attachment in anaerobic bacteria and provides a rationale for discriminating between type I and type II Coh modules.

Mechanism of bacterial cell-surface attachment revealed by the structure of cellulosomal type II cohesin-dockerin complex.,Adams JJ, Pal G, Jia Z, Smith SP Proc Natl Acad Sci U S A. 2006 Jan 10;103(2):305-10. Epub 2005 Dec 29. PMID:16384918^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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. 2006 Jan 10;103(2):305-10. Epub 2005 Dec 29. PMID:16384918

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2b59"

@@ Line 2: / Line 2: @@
 <StructureSection load='2b59' size='340' side='right' caption='[[2b59]], [[Resolution|resolution]] 2.11&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2b59]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Clostridium_thermocellum Clostridium thermocellum] and [http://en.wikipedia.org/wiki/Clostridium_thermocellum_atcc_27405 Clostridium thermocellum atcc 27405]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B59 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2B59 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2b59]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_27405 Atcc 27405] and [http://en.wikipedia.org/wiki/Cloth Cloth]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B59 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2B59 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SdbA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=203119 Clostridium thermocellum ATCC 27405]), cipA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1515 Clostridium thermocellum])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SdbA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=203119 CLOTH]), cipA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1515 ATCC 27405])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2b59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b59 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2b59 RCSB], [http://www.ebi.ac.uk/pdbsum/2b59 PDBsum], [http://www.topsan.org/Proteins/BSGI/2b59 TOPSAN]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2b59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b59 OCA], [http://pdbe.org/2b59 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2b59 RCSB], [http://www.ebi.ac.uk/pdbsum/2b59 PDBsum], [http://www.topsan.org/Proteins/BSGI/2b59 TOPSAN]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/CIPA_CLOTH CIPA_CLOTH]] Acts as a scaffolding protein in the cellulosome. It promotes binding of cellulose to the catalytic domains of the cellulolytic enzymes.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 25: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2b59" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Clostridium thermocellum]]
+[[Category: Atcc 27405]]
-[[Category: Clostridium thermocellum atcc 27405]]
+[[Category: Cloth]]
 [[Category: Adams, J J]]
 [[Category: Structural genomic]]

2b59

From Proteopedia

Revision as of 05:04, 10 September 2015

The type II cohesin dockerin complex

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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