6acf

<table><tr><td colspan='2'>[[6acf]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_stearothermophilus_10 Bacillus stearothermophilus 10]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ACF OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6ACF FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GT50_15010 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272567 Bacillus stearothermophilus 10])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6acf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6acf OCA], [http://pdbe.org/6acf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6acf RCSB], [http://www.ebi.ac.uk/pdbsum/6acf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6acf ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Leucine dehydrogenase (LDH, EC 1.4.1.9) is a NAD(+)-dependent oxidoreductase that catalyzes the deamination of branched-chain l-amino acids (BCAAs). LDH of Geobacillus stearothermophilus (GstLDH) is a highly thermostable enzyme that has been applied for the quantification or production of BCAAs. Here the cryo-electron microscopy (cryo-EM) structures of apo and NAD(+)-bound LDH are reported at 3.0 and 3.2A resolution, respectively. On comparing the structures, the two overall structures are almost identical, but it was observed that the partial conformational change was triggered by the interaction between Ser147 and the nicotinamide moiety of NAD(+). NAD(+) binding also enhanced the strength of oligomerization interfaces formed by the core domains. Such additional interdomain interaction is in good agreement with our experimental results showing that the residual activity of NAD(+)-bound form was approximately three times higher than that of the apo form after incubation at 80 degrees C. In addition, sequence comparison of three structurally known LDHs indicated a set of candidates for site-directed mutagenesis to improve thermostability. Subsequent mutation analysis actually revealed that non-conserved residues, including Ala94, Tyr127, and the C-terminal region, are crucial for oligomeric thermostability.

Structural insights into thermostabilization of leucine dehydrogenase from its atomic structure by cryo-electron microscopy.,Yamaguchi H, Kamegawa A, Nakata K, Kashiwagi T, Mizukoshi T, Fujiyoshi Y, Tani K J Struct Biol. 2018 Dec 10. pii: S1047-8477(18)30314-9. doi:, 10.1016/j.jsb.2018.12.001. PMID:30543982<ref>PMID:30543982</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 6acf" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Bacillus stearothermophilus 10]]

[[Category: Fujiyoshi, Y]]

[[Category: Kamegawa, A]]

[[Category: Kashiwagi, T]]

[[Category: Mizukoshi, T]]

[[Category: Nakata, K]]

[[Category: Tani, K]]

[[Category: Yamaguchi, H]]

[[Category: Oxidoreductase]]