4v40: Difference between revisions

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 == Structural highlights ==
 <table><tr><td colspan='2'>[[4v40]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1bgl 1bgl] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1bgm 1bgm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V40 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V40 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.5&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=4v40 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v40 OCA], [https://pdbe.org/4v40 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v40 RCSB], [https://www.ebi.ac.uk/pdbsum/4v40 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v40 ProSAT]</span></td></tr>
 </table>
 == Function ==
 [https://www.uniprot.org/uniprot/BGAL_ECOLI BGAL_ECOLI]
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The beta-galactosidase from Escherichia coli was instrumental in the development of the operon model, and today is one of the most commonly used enzymes in molecular biology. Here we report the structure of this protein and show that it is a tetramer with 222-point symmetry. The 1,023-amino-acid polypeptide chain folds into five sequential domains, with an extended segment at the amino terminus. The participation of this amino-terminal segment in a subunit interface, coupled with the observation that each active site is made up of elements from two different subunits, provides a structural rationale for the phenomenon of alpha-complementation. The structure represents the longest polypeptide chain for which an atomic structure has been determined. Our results show that it is possible successfully to study non-viral protein crystals with unit cell dimensions in excess of 500 A and with relative molecular masses in the region of 2,000K per asymmetric unit. Non-crystallographic symmetry averaging proved to be a very powerful tool in the structure determination, as has been shown in other contexts.
-Three-dimensional structure of beta-galactosidase from E. coli.,Jacobson RH, Zhang XJ, DuBose RF, Matthews BW Nature. 1994 Jun 30;369(6483):761-6. PMID:8008071<ref>PMID:8008071</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4v40" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Galactosidase 3D structures|Galactosidase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>