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| | <StructureSection load='3p3a' size='340' side='right'caption='[[3p3a]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='3p3a' size='340' side='right'caption='[[3p3a]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3p3a]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_19527 Atcc 19527]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3P3A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3P3A FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3p3a]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_thermoresistibile Mycolicibacterium thermoresistibile]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3P3A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3P3A FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3hzu|3hzu]]</div></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]] 2.1Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NODE_3859_LENGTH_3444_COV_7.617015_22 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1797 ATCC 19527])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Thiosulfate_sulfurtransferase Thiosulfate sulfurtransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.8.1.1 2.8.1.1] </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=3p3a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p3a OCA], [https://pdbe.org/3p3a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3p3a RCSB], [https://www.ebi.ac.uk/pdbsum/3p3a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3p3a 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=3p3a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p3a OCA], [https://pdbe.org/3p3a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3p3a RCSB], [https://www.ebi.ac.uk/pdbsum/3p3a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3p3a ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/E2QRA0_MYCTH E2QRA0_MYCTH] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 19527]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Thiosulfate sulfurtransferase]] | + | [[Category: Mycolicibacterium thermoresistibile]] |
| - | [[Category: Structural genomic]]
| + | |
| - | [[Category: Paratuberculosis]]
| + | |
| - | [[Category: Rhodanese]]
| + | |
| - | [[Category: Ssgcid]]
| + | |
| - | [[Category: Thermostable]]
| + | |
| - | [[Category: Thiosulfate cyanide transsulfurase]]
| + | |
| - | [[Category: Thiosulfate thiotransferase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Tuberculosis]]
| + | |
| Structural highlights
Function
E2QRA0_MYCTH
Publication Abstract from PubMed
The genus Mycobacterium comprises major human pathogens such as the causative agent of tuberculosis, Mycobacterium tuberculosis (Mtb), and many environmental species. Tuberculosis claims approximately 1.5 million lives every year, and drug resistant strains of Mtb are rapidly emerging. To aid the development of new tuberculosis drugs, major efforts are currently under way to determine crystal structures of Mtb drug targets and proteins involved in pathogenicity. However, a major obstacle to obtaining crystal structures is the generation of well-diffracting crystals. Proteins from thermophiles can have better crystallization and diffraction properties than proteins from mesophiles, but their sequences and structures are often divergent. Here, we establish a thermophilic mycobacterial model organism, Mycobacterium thermoresistibile (Mth), for the study of Mtb proteins. Mth tolerates higher temperatures than Mtb or other environmental mycobacteria such as M. smegmatis. Mth proteins are on average more soluble than Mtb proteins, and comparison of the crystal structures of two pairs of orthologous proteins reveals nearly identical folds, indicating that Mth structures provide good surrogates for Mtb structures. This study introduces a thermophile as a source of protein for the study of a closely related human pathogen and marks a new approach to solving challenging mycobacterial protein structures.
Mycobacterium thermoresistibile as a source of thermostable orthologs of Mycobacterium tuberculosis proteins.,Edwards TE, Liao R, Phan I, Myler PJ, Grundner C Protein Sci. 2012 Jul;21(7):1093-6. doi: 10.1002/pro.2084. Epub 2012 May 24. PMID:22544630[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Edwards TE, Liao R, Phan I, Myler PJ, Grundner C. Mycobacterium thermoresistibile as a source of thermostable orthologs of Mycobacterium tuberculosis proteins. Protein Sci. 2012 Jul;21(7):1093-6. doi: 10.1002/pro.2084. Epub 2012 May 24. PMID:22544630 doi:10.1002/pro.2084
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