1h7m: Difference between revisions

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 <StructureSection load='1h7m' size='340' side='right'caption='[[1h7m]], [[Resolution|resolution]] 1.96&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1h7m]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_35543 Atcc 35543]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H7M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H7M FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1h7m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_celer Thermococcus celer]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H7M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H7M FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1go0|1go0]], [[1go1|1go1]]</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]] 1.96&#8491;</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=1h7m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h7m OCA], [http://pdbe.org/1h7m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h7m RCSB], [http://www.ebi.ac.uk/pdbsum/1h7m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1h7m 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=1h7m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h7m OCA], [https://pdbe.org/1h7m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h7m RCSB], [https://www.ebi.ac.uk/pdbsum/1h7m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h7m ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/RL30E_THECE RL30E_THECE]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 17: / Line 19: @@
 </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=1h7m ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-We report here the high-resolution crystal structure of the ribosomal protein L30e from the hyperthermophilic archaeon Thermococcus celer determined at cryo-temperature. When it is compared with its mesophilic homologue, L30e from yeast, a number of structural features that can enhance thermostability are revealed. Disordered residues corresponding to a large RNA-binding loop in yeast L30e are well structured in the T. celer protein. The overall charge of T. celer L30e is near neutral, whereas that of the yeast homologue is highly positive. This is the result of an increase in the number of acidic residues at the expense of polar residues, Asn, Ser, and Thr. Extensive ion pair networks are found on the molecular surface. Exposed nonpolar surface areas are reduced in the T. celer protein. Its side chain atoms preferably form hydrogen bonds with main chain atoms. Taken together, these factors contribute to high protein stability. The roles of well-conserved L30e residues are studied and found to be important in defining a very compact overall structure and in maintaining the structure of the RNA binding site. By comparing it with the yeast homologue, we also identified the residues that are responsible for RNA binding and built a model to illustrate how L30e binds to an RNA kink turn motif.
-Crystal structure of ribosomal protein L30e from the extreme thermophile Thermococcus celer: thermal stability and RNA binding.,Chen YW, Bycroft M, Wong KB Biochemistry. 2003 Mar 18;42(10):2857-65. PMID:12627951<ref>PMID:12627951</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1h7m" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Kink-turn motif|Kink-turn motif]]
-*[[RNA motifs|RNA motifs]]
 *[[Ribosomal protein L30|Ribosomal protein L30]]
 *[[User:Wayne Decatur/kink-turn motif|User:Wayne Decatur/kink-turn motif]]
-*[[15.5kD/Snu13/L7Ae protein|15.5kD/Snu13/L7Ae protein]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Atcc 35543]]
 [[Category: Large Structures]]
-[[Category: Chen, Y W]]
+[[Category: Thermococcus celer]]
-[[Category: Wong, K B]]
+[[Category: Chen YW]]
-[[Category: Ribosomal protein]]
+[[Category: Wong KB]]
-[[Category: Ribosome]]
-[[Category: Rna-binding]]
-[[Category: Thermophilic]]