5dfm: Difference between revisions

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 ==Structure of Tetrahymena telomerase p19 fused to MBP==
-<StructureSection load='5dfm' size='340' side='right' caption='[[5dfm]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+<StructureSection load='5dfm' size='340' side='right'caption='[[5dfm]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5dfm]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DFM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DFM FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5dfm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Tetrahymena_thermophila Tetrahymena thermophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DFM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DFM FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAL:MALTOSE'>MAL</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]] 2.301&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5dfn|5dfn]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=5dfm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dfm OCA], [http://pdbe.org/5dfm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dfm RCSB], [http://www.ebi.ac.uk/pdbsum/5dfm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dfm 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=5dfm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dfm OCA], [https://pdbe.org/5dfm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dfm RCSB], [https://www.ebi.ac.uk/pdbsum/5dfm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dfm ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/MALE_ECO57 MALE_ECO57]] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides (By similarity).
+[https://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Telomerase helps maintain telomeres by processive synthesis of telomere repeat DNA at their 3'-ends, using an integral telomerase RNA (TER) and telomerase reverse transcriptase (TERT). We report the cryo-electron microscopy structure of Tetrahymena telomerase at ~9 angstrom resolution. In addition to seven known holoenzyme proteins, we identify two additional proteins that form a complex (TEB) with single-stranded telomere DNA-binding protein Teb1, paralogous to heterotrimeric replication protein A (RPA). The p75-p45-p19 subcomplex is identified as another RPA-related complex, CST (CTC1-STN1-TEN1). This study reveals the paths of TER in the TERT-TER-p65 catalytic core and single-stranded DNA exit; extensive subunit interactions of the TERT essential N-terminal domain, p50, and TEB; and other subunit identities and structures, including p19 and p45C crystal structures. Our findings provide structural and mechanistic insights into telomerase holoenzyme function.
-Structure of Tetrahymena telomerase reveals previously unknown subunits, functions, and interactions.,Jiang J, Chan H, Cash DD, Miracco EJ, Ogorzalek Loo RR, Upton HE, Cascio D, O'Brien Johnson R, Collins K, Loo JA, Zhou ZH, Feigon J Science. 2015 Oct 30;350(6260):aab4070. doi: 10.1126/science.aab4070. Epub 2015, Oct 15. PMID:26472759<ref>PMID:26472759</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 5dfm" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Telomerase-associated protein|Telomerase-associated protein]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Cascio, D]]
+[[Category: Escherichia coli]]
-[[Category: Chan, H]]
+[[Category: Large Structures]]
-[[Category: Feigon, J]]
+[[Category: Tetrahymena thermophila]]
-[[Category: Sawaya, M R]]
+[[Category: Cascio D]]
-[[Category: Cst complex]]
+[[Category: Chan H]]
-[[Category: Nuclear protein]]
+[[Category: Feigon J]]
-[[Category: Ob-fold]]
+[[Category: Sawaya MR]]
-[[Category: Oligonucleotide binding fold]]
-[[Category: P19]]
-[[Category: Telomerase]]
-[[Category: Ten1]]