5g2p: Difference between revisions

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'''Unreleased structure'''


The entry 5g2p is ON HOLD  until Paper Publication
==The crystal structure of a S-selective transaminase from Arthrobacter sp.==
<StructureSection load='5g2p' size='340' side='right' caption='[[5g2p]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5g2p]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5G2P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5G2P FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5g2q|5g2q]]</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5g2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g2p OCA], [http://pdbe.org/5g2p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5g2p RCSB], [http://www.ebi.ac.uk/pdbsum/5g2p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5g2p ProSAT]</span></td></tr>
</table>
<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 Arthrobacter sp.
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 5g2p" style="background-color:#fffaf0;"></div>
[[Category: Van Oosterwijk, N]]
== References ==
[[Category: Dijkstra, B.W]]
<references/>
__TOC__
</StructureSection>
[[Category: Dijkstra, B W]]
[[Category: Hekelaar, J]]
[[Category: Hekelaar, J]]
[[Category: Oosterwijk, N van]]
[[Category: Scheltinga, A C.Terwisscha van]]
[[Category: Turner, N J]]
[[Category: Willies, S]]
[[Category: Willies, S]]
[[Category: Turner, N.J]]
[[Category: Transaminase]]
[[Category: Transferase]]
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