4hcw: Difference between revisions

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 == Structural highlights ==
 <table><tr><td colspan='2'>[[4hcw]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Naegleria_gruberi Naegleria gruberi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HCW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HCW FirstGlance]. <br>
-</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=4hcw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hcw OCA], [https://pdbe.org/4hcw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hcw RCSB], [https://www.ebi.ac.uk/pdbsum/4hcw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hcw ProSAT]</span></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]] 2.705&#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=4hcw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hcw OCA], [https://pdbe.org/4hcw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hcw RCSB], [https://www.ebi.ac.uk/pdbsum/4hcw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hcw ProSAT]</span></td></tr>
 </table>
 == Function ==
 [https://www.uniprot.org/uniprot/D2V4Z5_NAEGR D2V4Z5_NAEGR]
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Thiaminases, enzymes that cleave vitamin B1, are sporadically distributed among prokaryotes and eukaryotes. Thiaminase I enzymes catalyze the elimination of the thiazole ring moiety from thiamin through substitution of the methylene group with a nitrogenous base or sulfhydryl compound. In eukaryotic organisms, these enzymes are reported to have much higher molecular weights than their bacterial counterparts. A thiaminase I of the single-celled amoeboflagellate Naegleria gruberi is the only eukaryotic thiaminase I to have been cloned, sequenced, and expressed. Here, we present the crystal structure of N. gruberi thiaminase I to a resolution of 2.8 A, solved by isomorphous replacement and pseudo-two-wavelength multiwavelength anomalous diffraction and refined to an R factor of 0.231 (Rfree, 0.265). This structure was used to solve the structure of the enzyme in complex with 3-deazathiamin, a noncleavable thiamin analog and enzyme inhibitor (2.7 A; R, 0.233; Rfree, 0.267). These structures define the mode of thiamin binding to this class of thiaminases and indicate the involvement of Asp272 as the catalytic base. This enzyme is able to use thiamin as a substrate and is active with amines such as aniline and veratrylamine as well as sulfhydryl compounds such as l-cysteine and beta-mercaptoethanol as cosubstrates. Despite significant differences in polypeptide sequence and length, we have shown that the N. gruberi thiaminase I is homologous in structure and activity to a previously characterized bacterial thiaminase I.
-Structure of a eukaryotic thiaminase I.,Kreinbring CA, Remillard SP, Hubbard P, Brodkin HR, Leeper FJ, Hawksley D, Lai EY, Fulton C, Petsko GA, Ringe D Proc Natl Acad Sci U S A. 2014 Jan 7;111(1):137-42. doi: 10.1073/pnas.1315882110., Epub 2013 Dec 18. PMID:24351929<ref>PMID:24351929</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4hcw" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Thiaminase|Thiaminase]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>