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==NMR SOLUTION STRUCTURE OF THE LAST UNKNOWN MODULE OF THE CELLULOSOMAL SCAFFOLDIN PROTEIN CIPC OF CLOSTRIDUM CELLULOLYTICUM==
==NMR SOLUTION STRUCTURE OF THE LAST UNKNOWN MODULE OF THE CELLULOSOMAL SCAFFOLDIN PROTEIN CIPC OF CLOSTRIDUM CELLULOLYTICUM==
<StructureSection load='1ehx' size='340' side='right'caption='[[1ehx]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='1ehx' size='340' side='right'caption='[[1ehx]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1ehx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_cellulolyticum Clostridium cellulolyticum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EHX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EHX FirstGlance]. <br>
<table><tr><td colspan='2'>[[1ehx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ruminiclostridium_cellulolyticum Ruminiclostridium cellulolyticum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EHX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EHX FirstGlance]. <br>
</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=1ehx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ehx OCA], [https://pdbe.org/1ehx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ehx RCSB], [https://www.ebi.ac.uk/pdbsum/1ehx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ehx ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1ehx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ehx OCA], [https://pdbe.org/1ehx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ehx RCSB], [https://www.ebi.ac.uk/pdbsum/1ehx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ehx ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q45996_9FIRM Q45996_9FIRM]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1ehx 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=1ehx ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Multidimensional, homo- and heteronuclear magnetic resonance spectroscopy combined with dynamical annealing has been used to determine the structure of a 94 residue module (X2 1) of the scaffolding protein CipC from the anaerobic bacterium Clostridium cellulolyticum. An experimental data set comprising 1647 nuclear Overhauser effect-derived restraints, 105 hydrogen bond restraints and 66 phi torsion angle restraints was used to calculate 20 converging final solutions. The calculated structures have an average rmsd about the mean structure of 0.55(+/-0.11) A for backbone atoms and 1.40(+/-0.11) A for all heavy atoms when fitted over the secondary structural elements. The X2 1 module has an immunoglobulin-like fold with two beta-sheets packed against each other. One sheet contains three strands, the second contains four strands. An additional strand is intercalated between the beta-sandwich, as well as two turns of a 3(.10) helix. X2 1 has a surprising conformational stability and may act as a conformational linker and solubility enhancer within the scaffolding protein. The fold of X2 1 is very similar to that of telokin, titin Ig domain, hemolin D2 domain, twitchin immunoglobulin domain and the first four domains of the IgSF portion of transmembrane cell adhesion molecule. As a consequence, the X2 1 module is the first prokaryotic member assigned to the I set of the immunoglobulin superfamily even though no sequence similarity with any member of this superfamily could be detected.
Solution structure of the module X2 1 of unknown function of the cellulosomal scaffolding protein CipC of Clostridium cellulolyticum.,Mosbah A, Belaich A, Bornet O, Belaich JP, Henrissat B, Darbon H J Mol Biol. 2000 Nov 24;304(2):201-17. PMID:11080456<ref>PMID:11080456</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1ehx" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Cellulosome scaffolding protein 3D structures|Cellulosome scaffolding protein 3D structures]]
*[[Cellulosome scaffolding protein 3D structures|Cellulosome scaffolding protein 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Clostridium cellulolyticum]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Belaich, A]]
[[Category: Ruminiclostridium cellulolyticum]]
[[Category: Belaich, J P]]
[[Category: Belaich A]]
[[Category: Bornet, O]]
[[Category: Belaich JP]]
[[Category: Darbon, H]]
[[Category: Bornet O]]
[[Category: Henrissat, B]]
[[Category: Darbon H]]
[[Category: Mosbah, A]]
[[Category: Henrissat B]]
[[Category: 10 helix]]
[[Category: Mosbah A]]
[[Category: Beta-beta-barrel]]
[[Category: Unknown function]]

Revision as of 13:02, 20 March 2024

NMR SOLUTION STRUCTURE OF THE LAST UNKNOWN MODULE OF THE CELLULOSOMAL SCAFFOLDIN PROTEIN CIPC OF CLOSTRIDUM CELLULOLYTICUMNMR SOLUTION STRUCTURE OF THE LAST UNKNOWN MODULE OF THE CELLULOSOMAL SCAFFOLDIN PROTEIN CIPC OF CLOSTRIDUM CELLULOLYTICUM

Structural highlights

1ehx is a 1 chain structure with sequence from Ruminiclostridium cellulolyticum. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q45996_9FIRM

Evolutionary Conservation

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

See Also

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OCA
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