1dcj: Difference between revisions

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-{{Seed}}
-[[Image:1dcj.png|left|200px]]
-<!--
+==SOLUTION STRUCTURE OF YHHP, A NOVEL ESCHERICHIA COLI PROTEIN IMPLICATED IN THE CELL DIVISION==
-The line below this paragraph, containing "STRUCTURE_1dcj", creates the "Structure Box" on the page.
+<StructureSection load='1dcj' size='340' side='right'caption='[[1dcj]]' 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'>[[1dcj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DCJ 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">Solution NMR</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=1dcj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dcj OCA], [https://pdbe.org/1dcj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dcj RCSB], [https://www.ebi.ac.uk/pdbsum/1dcj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dcj ProSAT]</span></td></tr>
-{{STRUCTURE_1dcj|  PDB=1dcj  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/TUSA_ECOLI TUSA_ECOLI] Part of a sulfur-relay system required for 2-thiolation of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions. Interacts with IscS and stimulates its activity. Then, accepts a sulfur from IscS and transfers it in turn to TusD. Seems to affect the stability of sigma-S, particularly during the logarithmic growth phase.<ref>PMID:16387657</ref>
+== 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/dc/1dcj_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1dcj ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+YhhP, a small protein of 81 amino acid residues encoded by the yhhP gene in the Escherichia coli database, is implicated in cell division although the precise biological function of this protein has not been yet identified. A variety of microorganisms have similar proteins, all of which contain a common CPxP sequence motif in the N-terminal region. We have determined the three-dimensional solution structure of YhhP by NMR spectroscopy in order to obtain insight into its biological function. It folds into a two-layered alpha/beta-sandwich structure with a betaalphabetaalphabetabeta fold, comprising a mixed four-stranded beta-sheet stacked against two alpha-helices, both of which are nearly parallel to the strands of the beta-sheet. The CPxP motif plays a significant structural role in stabilizing the first helix as a part of the new type N-capping box where the Cys-Pro peptide bond adopts a cis configuration. The structure of YhhP displays a striking resemblance to the C-terminal ribosome-binding domain of translation initiation factor IF3 (IF3C). In addition, the surface charge distribution of the RNA-recognition helix of IF3C is nearly the same as that of the corresponding helix of YhhP. These results suggest a structure-based hypothesis in which binding to an RNA target plays an essential role in the function of this ubiquitous protein.
-===SOLUTION STRUCTURE OF YHHP, A NOVEL ESCHERICHIA COLI PROTEIN IMPLICATED IN THE CELL DIVISION===
+High precision NMR structure of YhhP, a novel Escherichia coli protein implicated in cell division.,Katoh E, Hatta T, Shindo H, Ishii Y, Yamada H, Mizuno T, Yamazaki T J Mol Biol. 2000 Nov 24;304(2):219-29. PMID:11080457<ref>PMID:11080457</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_11080457}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1dcj" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 11080457 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_11080457}}
+__TOC__
+</StructureSection>
-==About this Structure==
-DCJ is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCJ OCA].
-==Reference==
-<ref group="xtra">PMID:11080457</ref><references group="xtra"/>
 [[Category: Escherichia coli]]
-[[Category: Hatta, T.]]
+[[Category: Large Structures]]
-[[Category: Katoh, E.]]
+[[Category: Hatta T]]
-[[Category: Mizuno, T.]]
+[[Category: Katoh E]]
-[[Category: Shindo, H.]]
+[[Category: Mizuno T]]
-[[Category: Yamazaki, T.]]
+[[Category: Shindo H]]
-[[Category: Alpha-beta sandwich]]
+[[Category: Yamazaki T]]
-[[Category: Structural genomic]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 22:34:15 2009''