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==The type II cohesin dockerin complex==
==The type II cohesin dockerin complex==
<StructureSection load='2b59' size='340' side='right' caption='[[2b59]], [[Resolution|resolution]] 2.11&Aring;' scene=''>
<StructureSection load='2b59' size='340' side='right'caption='[[2b59]], [[Resolution|resolution]] 2.11&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<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>
<table><tr><td colspan='2'>[[2b59]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acetivibrio_thermocellus Acetivibrio thermocellus] and [https://en.wikipedia.org/wiki/Acetivibrio_thermocellus_ATCC_27405 Acetivibrio thermocellus 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 [https://proteopedia.org/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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.11&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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://prosat.h-its.org/prosat/prosatexe?pdbcode=2b59 ProSAT], [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'>[https://proteopedia.org/fgij/fg.htm?mol=2b59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b59 OCA], [https://pdbe.org/2b59 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b59 RCSB], [https://www.ebi.ac.uk/pdbsum/2b59 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b59 ProSAT], [https://www.topsan.org/Proteins/BSGI/2b59 TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== 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.
[https://www.uniprot.org/uniprot/A3DF10_ACET2 A3DF10_ACET2]  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b5/2b59_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b5/2b59_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
Line 20: Line 20:
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2b59 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2b59 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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<ref>PMID:16384918</ref>
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>


==See Also==
==See Also==
*[[Cellulosomal scaffolding protein A|Cellulosomal scaffolding protein A]]
*[[Cellulosome scaffolding protein 3D structures|Cellulosome scaffolding protein 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 27405]]
[[Category: Acetivibrio thermocellus]]
[[Category: Cloth]]
[[Category: Acetivibrio thermocellus ATCC 27405]]
[[Category: Adams, J J]]
[[Category: Large Structures]]
[[Category: Structural genomic]]
[[Category: Adams JJ]]
[[Category: Smith, S P]]
[[Category: Smith SP]]
[[Category: Bsgi]]
[[Category: Cellulosome]]
[[Category: Ef hand]]
[[Category: Hydrolase-structural protein complex]]
[[Category: Protein-protein complex]]

Latest revision as of 12:16, 14 February 2024

The type II cohesin dockerin complexThe type II cohesin dockerin complex

Structural highlights

2b59 is a 2 chain structure with sequence from Acetivibrio thermocellus and Acetivibrio thermocellus ATCC 27405. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.11Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

A3DF10_ACET2

Evolutionary Conservation

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

See Also

2b59, resolution 2.11Å

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