3itw: Difference between revisions

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-{{Seed}}
-[[Image:3itw.jpg|left|200px]]
-<!--
+==Crystal structure of TioX from Micromonospora sp. ML1==
-The line below this paragraph, containing "STRUCTURE_3itw", creates the "Structure Box" on the page.
+<StructureSection load='3itw' size='340' side='right'caption='[[3itw]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3itw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Micromonospora_sp._ML1 Micromonospora sp. ML1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ITW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ITW FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</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=3itw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3itw OCA], [https://pdbe.org/3itw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3itw RCSB], [https://www.ebi.ac.uk/pdbsum/3itw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3itw ProSAT]</span></td></tr>
-{{STRUCTURE_3itw|  PDB=3itw  |  SCENE=  }}
+</table>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/it/3itw_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3itw ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Thiocoraline is a thiodepsipeptide with potent antitumor activity. TioX, a protein with an unidentified function, is encoded by a gene of the thiocoraline biosynthetic gene cluster. The crystal structure of the full-length TioX protein at 2.15 A resolution reveals that TioX protomer shares an ancient betaalphabetabetabeta fold motif with glyoxalase I and bleomycin resistance protein families, despite a very low sequence homology. Intriguingly, four TioX monomers form a unique 2-fold symmetric tetrameric assembly that is stabilized by four intermolecular disulfide bonds formed cyclically between Cys60 and Cys66 of adjacent monomers. The arrangement of two of the four monomers in the TioX tetramer is analogous to that in dimeric bleomycin resistance proteins. This analogy indicates that this novel higher-order structural scaffold of TioX may have evolved to bind thiocoraline. Our equilibrium titration studies demonstrate the binding of a thiocoraline chromophore analog, quinaldic acid, to TioX, thereby substantiating this model. Furthermore, a strain of Streptomyces albus containing an exogenous thiocoraline gene cluster devoid of functional tioX maintains thiocoraline production, albeit with a lower yield. Taken together, these observations rule out a direct enzymatic function of TioX and suggest that TioX is involved in thiocoraline resistance or secretion.
-===Crystal structure of TioX from Micromonospora sp. ML1===
+A new scaffold of an old protein fold ensures binding to the bisintercalator thiocoraline.,Biswas T, Zolova OE, Lombo F, de la Calle F, Salas JA, Tsodikov OV, Garneau-Tsodikova S J Mol Biol. 2010 Mar 26;397(2):495-507. Epub 2010 Feb 1. PMID:20122935<ref>PMID:20122935</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_20122935}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 3itw" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 20122935 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_20122935}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-ITW is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Micromonospora_sp._ml1 Micromonospora sp. ml1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ITW OCA].
+[[Category: Micromonospora sp. ML1]]
+[[Category: Biswas T]]
-==Reference==
+[[Category: Garneau-Tsodikova S]]
-<ref group="xtra">PMID:20122935</ref><references group="xtra"/>
+[[Category: Tsodikov OV]]
-[[Category: Micromonospora sp. ml1]]
-[[Category: Biswas, T.]]
-[[Category: Garneau-Tsodikova, S.]]
-[[Category: Tsodikov, O V.]]
-[[Category: Bisintercalator]]
-[[Category: Bleomycin resistance fold]]
-[[Category: Peptide binding protein]]
-[[Category: Protein binding]]
-[[Category: Solvent-exposed trp residue]]
-[[Category: Thiocoraline]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 17 10:31:26 2010''