8dko
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Minimal PutA proline dehydrogenase domain (design #1) complexed with S-(-)-tetrahydro-2-furoic acid== | |
| + | <StructureSection load='8dko' size='340' side='right'caption='[[8dko]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8dko]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sinorhizobium_meliloti_SM11 Sinorhizobium meliloti SM11]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8DKO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DKO FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=TFB:TETRAHYDROFURAN-2-CARBOXYLIC+ACID'>TFB</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=8dko FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8dko OCA], [https://pdbe.org/8dko PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8dko RCSB], [https://www.ebi.ac.uk/pdbsum/8dko PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8dko ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/F7X6I3_SINMM F7X6I3_SINMM] Oxidizes proline to glutamate for use as a carbon and nitrogen source.[PIRNR:PIRNR000197] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Proline dehydrogenase (PRODH) catalyzes the FAD-dependent oxidation of L-proline to Delta1-pyrroline-5-carboxylate and is a target for inhibitor discovery because of its importance in cancer cell metabolism. Because human PRODH is challenging to purify, the PRODH domains of the bacterial bifunctional enzyme proline utilization A (PutA) have been used for inhibitor development. These systems have limitations due to large polypeptide chain length, conformational flexibility, and the presence of domains unrelated to PRODH activity. Herein, we report the engineering of minimal PRODH domains for inhibitor discovery. The best designs contain about one-third of the 1233-residue parent PutA from Sinorhizobium meliloti and include an artificial linker that replaces the PutA alpha-domain. The minimal PRODHs exhibit near wild-type enzymatic activity and are susceptible to known reversible inhibitors and covalent inactivators. Crystal structures of minimal PRODHs inhibited by S-(-)-tetrahydro-2-furoic acid and 2-(furan-2-yl)acetic acid were determined at 1.23 and 1.72 A resolution, respectively. Minimal PRODHs should be useful in chemical probe discovery. | ||
| - | + | Structure-based engineering of minimal Proline dehydrogenase domains for inhibitor discovery.,Bogner AN, Ji J, Tanner JJ Protein Eng Des Sel. 2022 Nov 30:gzac016. doi: 10.1093/protein/gzac016. PMID:36448708<ref>PMID:36448708</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Bogner | + | <div class="pdbe-citations 8dko" style="background-color:#fffaf0;"></div> |
| - | [[Category: Tanner | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Sinorhizobium meliloti SM11]] | ||
| + | [[Category: Bogner AN]] | ||
| + | [[Category: Tanner JJ]] | ||
Revision as of 10:10, 14 December 2022
Minimal PutA proline dehydrogenase domain (design #1) complexed with S-(-)-tetrahydro-2-furoic acid
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