7p3t: Difference between revisions

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New page: '''Unreleased structure''' The entry 7p3t is ON HOLD Authors: Ermler, U., Ermler, U. Description: Transaminase of gamma-proteobacterium Category: Unreleased Structures [[Category: ...
 
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'''Unreleased structure'''


The entry 7p3t is ON HOLD
==Transaminase of gamma-proteobacterium==
<StructureSection load='7p3t' size='340' side='right'caption='[[7p3t]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7p3t]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Luminiphilus_syltensis_NOR5-1B Luminiphilus syltensis NOR5-1B]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7P3T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7P3T 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]] 1.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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=7p3t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7p3t OCA], [https://pdbe.org/7p3t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7p3t RCSB], [https://www.ebi.ac.uk/pdbsum/7p3t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7p3t ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B8KQT8_9GAMM B8KQT8_9GAMM]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Despite the plethora of information on (S)-selective amine transaminases, the (R)-selective ones are still not well-studied; only a few structures are known to date, and their substrate scope is limited, apart from a few stellar works in the field. Herein, the structure of Luminiphilus syltensis (R)-selective amine transaminase is elucidated to facilitate engineering towards variants active on bulkier substrates. The V37A variant exhibited increased activity towards 1-phenylpropylamine and to activity against 1-butylamine. In contrast, the S248 and T249 positions, located on the beta-turn in the P-pocket, seem crucial for maintaining the activity of the enzyme.


Authors: Ermler, U., Ermler, U.
Rational engineering of Luminiphilus syltensis (R)-selective amine transaminase for the acceptance of bulky substrates.,Konia E, Chatzicharalampous K, Drakonaki A, Muenke C, Ermler U, Tsiotis G, Pavlidis IV Chem Commun (Camb). 2021 Dec 3;57(96):12948-12951. doi: 10.1039/d1cc04664k. PMID:34806715<ref>PMID:34806715</ref>


Description: Transaminase of gamma-proteobacterium
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Ermler, U]]
<div class="pdbe-citations 7p3t" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Aminotransferase 3D structures|Aminotransferase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Luminiphilus syltensis NOR5-1B]]
[[Category: Ermler U]]
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