3tk1: Difference between revisions

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 ==Crystal structure of a MeaB and Rv1496 ortholog from Mycobacterium thermoresistible bound to GDP==
-<StructureSection load='3tk1' size='340' side='right' caption='[[3tk1]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+<StructureSection load='3tk1' size='340' side='right'caption='[[3tk1]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3tk1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_thermoresistibile_atcc_19527 Mycobacterium thermoresistibile atcc 19527]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TK1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TK1 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3tk1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_thermoresistibile_ATCC_19527 Mycolicibacterium thermoresistibile ATCC 19527]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TK1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TK1 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</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]] 2.4&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3md0|3md0]], [[3p32|3p32]], [[3nxs|3nxs]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KEK_00260 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1078020 Mycobacterium thermoresistibile ATCC 19527])</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=3tk1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tk1 OCA], [https://pdbe.org/3tk1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tk1 RCSB], [https://www.ebi.ac.uk/pdbsum/3tk1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tk1 ProSAT]</span></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=3tk1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tk1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tk1 RCSB], [http://www.ebi.ac.uk/pdbsum/3tk1 PDBsum]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/G7CAR0_MYCT3 G7CAR0_MYCT3]
-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<ref>PMID:22544630</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Mycobacterium thermoresistibile atcc 19527]]
+[[Category: Large Structures]]
-[[Category: Structural genomic]]
+[[Category: Mycolicibacterium thermoresistibile ATCC 19527]]
-[[Category: G-protein]]
-[[Category: Gdp]]
-[[Category: Hydrolase]]
-[[Category: Meab]]
-[[Category: Methylmalonic aciduria]]
-[[Category: Mmaa]]
-[[Category: Ras-like gtpase]]
-[[Category: Rv1496]]
-[[Category: Ssgcid]]
-[[Category: Thermophile]]