5g09: Difference between revisions

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'''Unreleased structure'''


The entry 5g09 is ON HOLD
==The crystal structure of a S-selective transaminase from Bacillus megaterium bound with R-alpha-methylbenzylamine==
<StructureSection load='5g09' size='340' side='right'caption='[[5g09]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5g09]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Priestia_megaterium Priestia megaterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5G09 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5G09 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]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=6DF:[6-METHYL-5-OXIDANYL-4-[(~{E})-[(1~{R})-1-PHENYLETHYL]IMINOMETHYL]PYRIDIN-3-YL]METHYL+DIHYDROGEN+PHOSPHATE'>6DF</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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=5g09 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g09 OCA], [https://pdbe.org/5g09 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5g09 RCSB], [https://www.ebi.ac.uk/pdbsum/5g09 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5g09 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A1C7D190_PRIMG A0A1C7D190_PRIMG]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
omega-Transaminases are enzymes that can introduce an amino group in industrially interesting compounds. We determined crystal structures of two (S)-selective omega-transaminases, one from Arthrobacter sp. (Ars-omegaTA) and one from Bacillus megaterium (BM-omegaTA), which have 95% sequence identity, but somewhat different activity profiles. Substrate-profiling measurements using a range of (R)- and (S)-substrates showed that both enzymes have a preference for substrates with large planar side groups for which the activity of BM-omegaTA is generally somewhat higher. BM-omegaTA has a significantly higher preference for (S)-3,3-dimethyl-2-butylamine than Ars-omegaTA, as well as a more relaxed enantiopreference towards 1-cyclopropylethylamine. The crystal structures showed that, as expected for (S)-selective transaminases, both enzymes have the typical transaminase type I fold, and have spacious active sites to accommodate largish substrates. A structure of BM-omegaTA with bound (R)-alpha-methylbenzylamine explains the enzymes' preference for (S)-substrates. Site-directed mutagenesis experiments revealed that the presence of a tyrosine instead of a cysteine at position 60 increases the relative activities on several small substrates. A structure of Ars-omegaTA with bound L-Ala revealed that the Arg442 side chain has repositioned to bind the L-Ala carboxylate. Compared to the arginine switch residue in other transaminases, Arg442 is shifted by six residues in the amino acid sequence, which appears to be a consequence of extra loops near the active site that narrow the entrance to the active site.


Authors: van Oosterwijk, N., Willies, S., Hekelaar, J., Terwisscha van Scheltinga, A.C., Turner, N.J., Dijkstra, B.W.
Structural basis of substrate range and enantioselectivity of two (S)-selective omega-transaminases.,van Oosterwijk N, Willies SC, Hekelaar J, Terwisscha van Scheltinga AC, Turner NJ, Dijkstra BW Biochemistry. 2016 Jul 18. PMID:27428867<ref>PMID:27428867</ref>


Description: The crystal structure of a S-selective transaminase from Bacillus megaterium bound with R-alpha-methylbenzylamine
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Terwisscha Van Scheltinga, A.C]]
<div class="pdbe-citations 5g09" style="background-color:#fffaf0;"></div>
[[Category: Van Oosterwijk, N]]
== References ==
[[Category: Dijkstra, B.W]]
<references/>
[[Category: Hekelaar, J]]
__TOC__
[[Category: Willies, S]]
</StructureSection>
[[Category: Turner, N.J]]
[[Category: Large Structures]]
[[Category: Priestia megaterium]]
[[Category: Dijkstra BW]]
[[Category: Hekelaar J]]
[[Category: Terwisscha van Scheltinga AC]]
[[Category: Turner NJ]]
[[Category: Willies S]]
[[Category: Van Oosterwijk N]]
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