View source for 4xlx


==Crystal structure of BjKS from Bradyrhizobium japonicum==
<StructureSection load='4xlx' size='340' side='right'caption='[[4xlx]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4xlx]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bradyrhizobium_diazoefficiens_USDA_110 Bradyrhizobium diazoefficiens USDA 110]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XLX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XLX FirstGlance]. <br>
</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&#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=4xlx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xlx OCA], [https://pdbe.org/4xlx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xlx RCSB], [https://www.ebi.ac.uk/pdbsum/4xlx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xlx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Y2150_BRADU Y2150_BRADU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We report the first X-ray crystal structure of ent-kaur-16-ene synthase from Bradyrhizobium japonicum, together with the results of a site-directed mutagenesis investigation into catalytic activity. The structure is very similar to that of the alpha domains of modern plant terpene cyclases, a result that is of interest since it has been proposed that many plant terpene cyclases may have arisen from bacterial diterpene cyclases. The ent-copalyl diphosphate substrate binds to a hydrophobic pocket near a cluster of Asp and Arg residues that are essential for catalysis, with the carbocations formed on ionization being protected by Leu, Tyr and Phe residues. A bisphosphonate inhibitor binds to the same site. In the kaurene synthase from the moss Physcomitrella patens, 16-alpha-hydroxy-ent-kaurane as well as kaurene are produced since Leu and Tyr in the P. patens kaurene synthase active site are replaced by smaller residues enabling carbocation quenching by water. Overall, the results represent the first structure determination of a bacterial diterpene cyclase, providing insights into catalytic activity, as well as structural comparisons with diverse terpene synthases and cyclases which clearly separate the terpene cyclases from other terpene synthases having highly alpha-helical structures.

Structure, function and inhibition of ent-kaurene synthase from Bradyrhizobium japonicum.,Liu W, Feng X, Zheng Y, Huang CH, Nakano C, Hoshino T, Bogue S, Ko TP, Chen CC, Cui Y, Li J, Wang I, Hsu ST, Oldfield E, Guo RT Sci Rep. 2014 Oct 1;4:6214. doi: 10.1038/srep06214. PMID:25269599<ref>PMID:25269599</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4xlx" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bradyrhizobium diazoefficiens USDA 110]]
[[Category: Large Structures]]
[[Category: Guo RT]]
[[Category: Hu Y]]
[[Category: Ko TP]]
[[Category: Liu W]]
[[Category: Zheng Y]]