2kaa: Difference between revisions

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-{{Seed}}
-[[Image:2kaa.jpg|left|200px]]
-<!--
+==Solution Structure of Hirsutellin A from Hirsutella thompsonii==
-The line below this paragraph, containing "STRUCTURE_2kaa", creates the "Structure Box" on the page.
+<StructureSection load='2kaa' size='340' side='right'caption='[[2kaa]]' 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'>[[2kaa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hirsutella_thompsonii Hirsutella thompsonii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KAA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KAA 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, 20 models</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=2kaa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kaa OCA], [https://pdbe.org/2kaa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kaa RCSB], [https://www.ebi.ac.uk/pdbsum/2kaa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kaa ProSAT]</span></td></tr>
-{{STRUCTURE_2kaa|  PDB=2kaa  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/P78696_HIRTH P78696_HIRTH]
+== 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/ka/2kaa_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=2kaa ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Hirsutellin (HtA) is intermediate in size between other ribotoxins and less specific microbial RNases, and thus offers a unique chance to determine the minimal structural requirements for activities unique to ribotoxins. Here, we have determined the structure of HtA by NMR methods. The structure consists of one alpha-helix, a helical turn and seven beta-strands that form an N-terminal hairpin and an anti-parallel beta-sheet, with a characteristic alpha + beta fold and a highly positive charged surface. Compared to its larger homolog alpha-sarcin, the N-terminal hairpin is shorter and less positively charged. The secondary structure elements are connected by large loops with root mean square deviation (rmsd) values &gt; 1 A, suggesting some degree of intrinsically dynamic behavior. The active site architecture of HtA is unique among ribotoxins. Compared to alpha-sarcin, HtA has an aspartate group, D40, replacing a tyrosine, and the aromatic ring of F126, located in the leucine 'environment' close to the catalytic H113 in a similar arrangement to that found in RNase T1. This unique active site structure is discussed in terms of its novel electrostatic interactions to understand the efficient cytotoxic activity of HtA. The contributions of the N-terminal hairpin, loop 2 and loop 5 with regard to protein functionality, protein-protein and protein-ipid interactions, are also discussed. The truncation and reduced charge of the N-terminal hairpin in HtA may be compensated for by the extension and new orientation of its loop 5. This novel orientation of loop 5 re-establishes a positive charge on the side of the molecule that has been shown to be important for intermolecular interactions in ribotoxins.
-===Solution Structure of Hirsutellin A from Hirsutella thompsonii===
+Solution structure of hirsutellin A--new insights into the active site and interacting interfaces of ribotoxins.,Viegas A, Herrero-Galan E, Onaderra M, Macedo AL, Bruix M FEBS J. 2009 Apr;276(8):2381-90. PMID:19348010<ref>PMID:19348010</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_19348010}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 2kaa" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 19348010 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_19348010}}
+__TOC__
+</StructureSection>
-==About this Structure==
-KAA is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Hirsutella_thompsonii Hirsutella thompsonii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KAA OCA].
-==Reference==
-<ref group="xtra">PMID:19348010</ref><references group="xtra"/>
 [[Category: Hirsutella thompsonii]]
-[[Category: Bruix, M.]]
+[[Category: Large Structures]]
-[[Category: Macedo, A L.]]
+[[Category: Bruix M]]
-[[Category: Viegas, A.]]
+[[Category: Macedo AL]]
-[[Category: Alpha-sarcin]]
+[[Category: Viegas A]]
-[[Category: Hirsutella thompsonii]]
-[[Category: Hirsutellin some]]
-[[Category: Ribotoxin]]
-[[Category: Rip]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Nov  4 10:48:47 2009''