View source for 3x27


==Structure of McbB in complex with tryptophan==
<StructureSection load='3x27' size='340' side='right'caption='[[3x27]], [[Resolution|resolution]] 2.48&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3x27]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Marinactinospora_thermotolerans Marinactinospora thermotolerans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3X27 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3X27 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]] 2.481&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</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=3x27 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3x27 OCA], [https://pdbe.org/3x27 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3x27 RCSB], [https://www.ebi.ac.uk/pdbsum/3x27 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3x27 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/R4QPW9_9ACTN R4QPW9_9ACTN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The beta-carboline (betaC) alkaloids occur throughout nature and exhibit diverse biological activities. In contrast to betaC alkaloid synthesis in plants, the biosynthesis in microorganisms remains poorly understood. The recently reported McbB from Marinactinospora thermotolerans is a novel enzyme proposed to catalyze the Pictet-Spengler (PS) reaction of L-tryptophan and oxaloacetaldehyde to produce the betaC scaffold of marinacarbolines. In this study, we solved the crystal structure of McbB complexed with L-tryptophan at 2.48 A resolution, which revealed the novel protein folding of McbB and the totally different structure from those of other PS condensation catalyzing enzymes, such as strictosidine synthase and norcoclaurine synthase from plants. Structural analysis and site-directed mutagenesis confirmed that the previously proposed catalytic Glu97 at the active-site center functions as an acid and base catalyst. Remarkably, the structure-based mutants R72A and H87A, with expanded active-site cavities, newly accepted bulky phenylglyoxal as the aldehyde substrate, to produce 1-benzoyl-3-carboxy-beta-carboline.

Structural Basis for beta-Carboline Alkaloid Production by the Microbial Homodimeric Enzyme McbB.,Mori T, Hoshino S, Sahashi S, Wakimoto T, Matsui T, Morita H, Abe I Chem Biol. 2015 Jul 23;22(7):898-906. doi: 10.1016/j.chembiol.2015.06.006. Epub, 2015 Jun 25. PMID:26120001<ref>PMID:26120001</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3x27" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Marinactinospora thermotolerans]]
[[Category: Abe I]]
[[Category: Mori T]]
[[Category: Morita H]]
[[Category: Sahashi S]]