|
|
| Line 3: |
Line 3: |
| | <StructureSection load='3hzu' size='340' side='right'caption='[[3hzu]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='3hzu' size='340' side='right'caption='[[3hzu]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3hzu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HZU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HZU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3hzu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HZU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HZU FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.1Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3hwi|3hwi]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sseA, Rv3283, MT3382, MTCY71.23 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</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=3hzu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hzu OCA], [https://pdbe.org/3hzu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hzu RCSB], [https://www.ebi.ac.uk/pdbsum/3hzu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hzu 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=3hzu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hzu OCA], [https://pdbe.org/3hzu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hzu RCSB], [https://www.ebi.ac.uk/pdbsum/3hzu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hzu ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/THT2_MYCTU THT2_MYCTU] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 37: |
Line 37: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Thiosulfate sulfurtransferase]] | + | [[Category: Mycobacterium tuberculosis]] |
| - | [[Category: Structural genomic]]
| + | |
| - | [[Category: Infectious disease]]
| + | |
| - | [[Category: Niaid]]
| + | |
| - | [[Category: Ssgcid]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Tuberculosis]]
| + | |
| Structural highlights
Function
THT2_MYCTU
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
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
|
