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3o7o

From Proteopedia

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Current revision (10:03, 14 February 2024) (edit) (undo)
 
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<StructureSection load='3o7o' size='340' side='right'caption='[[3o7o]], [[Resolution|resolution]] 2.41&Aring;' scene=''>
<StructureSection load='3o7o' size='340' side='right'caption='[[3o7o]], [[Resolution|resolution]] 2.41&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3o7o]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O7O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O7O FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3o7o]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O7O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O7O FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.41&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TM1524, TM_1524 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene></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=3o7o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o7o OCA], [https://pdbe.org/3o7o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o7o RCSB], [https://www.ebi.ac.uk/pdbsum/3o7o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o7o ProSAT]</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=3o7o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o7o OCA], [https://pdbe.org/3o7o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o7o RCSB], [https://www.ebi.ac.uk/pdbsum/3o7o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o7o ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q9S5X8_THEMA Q9S5X8_THEMA]
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Protein crystallization continues to be a major bottleneck in X-ray crystallography. Previous studies suggest that symmetric proteins, such as homodimers, might crystallize more readily than monomeric proteins or asymmetric complexes. Proteins that are naturally monomeric can be made homodimeric artificially. Our approach is to create homodimeric proteins by introducing single cysteines into the protein of interest, which are then oxidized to form a disulfide bond between the two monomers. By introducing the single cysteine at different sequence positions, one can produce a variety of synthetically dimerized versions of a protein, with each construct expected to exhibit its own crystallization behavior. In earlier work, we demonstrated the potential utility of the approach using T4 lysozyme as a model system. Here we report the successful application of the method to Thermotoga maritima CelA, a thermophilic endoglucanase enzyme with low sequence identity to proteins with structures previously reported in the Protein Data Bank. This protein had resisted crystallization in its natural monomeric form, despite a broad survey of crystallization conditions. The synthetic dimerization of the CelA mutant D188C yielded well-diffracting crystals with molecules in a packing arrangement that would not have occurred with native, monomeric CelA. A 2.4 A crystal structure was determined by single anomalous dispersion using a seleno-methionine derivatized protein. The results support the notion that synthetic symmetrization can be a useful approach for enlarging the search space for crystallizing monomeric proteins or asymmetric complexes.To determine the atomic structure of a protein by X-ray diffraction, a crystal of the molecule must be grown. This remains a challenge for many proteins. We show that by creating multiple dimeric versions of a protein of interest - which can be done by engineering a disulfide bond between two copies of the molecule -additional opportunities are created for the protein to crystallize. The method is used to determine the structure of an endoglucanase enzyme.
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Use of synthetic symmetrization in the crystallization and structure determination of CelA from Thermotoga maritima.,Forse GJ, Ram N, Banatao DR, Cascio D, Sawaya MR, Klock HE, Lesley SA, Yeates TO Protein Sci. 2010 Nov 16. PMID:21082721<ref>PMID:21082721</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3o7o" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Glucanase 3D structures|Glucanase 3D structures]]
*[[Glucanase 3D structures|Glucanase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 43589]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Forse, G J]]
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[[Category: Thermotoga maritima]]
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[[Category: Ram, N]]
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[[Category: Forse GJ]]
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[[Category: Yeates, T O]]
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[[Category: Ram N]]
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[[Category: Disulfide bond]]
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[[Category: Yeates TO]]
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[[Category: Hydrolase]]
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[[Category: Lattice contact]]
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[[Category: Macromolecular crystallization]]
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[[Category: Oligomer]]
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[[Category: Protein design]]
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[[Category: Synthetic symmetrization]]
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Current revision

Use of synthetic symmetrization in the crystallization and structure determination of CelA from Thermotoga maritima

PDB ID 3o7o

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