6t3e
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==Structure of Thermococcus litoralis Delta(1)-pyrroline-2-carboxylate reductase in complex with NADH and L-proline== | |
+ | <StructureSection load='6t3e' size='340' side='right'caption='[[6t3e]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[6t3e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_litoralis_DSM_5473 Thermococcus litoralis DSM 5473]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T3E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6T3E 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]] 2.6Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</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=6t3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t3e OCA], [https://pdbe.org/6t3e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6t3e RCSB], [https://www.ebi.ac.uk/pdbsum/6t3e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6t3e ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/H3ZMH3_THELN H3ZMH3_THELN] | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | L-Hydroxyproline (L-Hyp) is a nonstandard amino acid that is present in certain proteins, in some antibiotics and in the cell-wall components of plants. L-Hyp is the product of the post-translational modification of protein prolines by prolyl hydroxylase enzymes, and the isomers trans-3-hydroxy-L-proline (T3LHyp) and trans-4-hydroxy-L-proline (T4LHyp) are major components of mammalian collagen. T4LHyp follows two distinct degradation pathways in bacteria and mammals, while T3LHyp is metabolized by a two-step metabolic pathway that is conserved in bacteria and mammals, which involves a T3LHyp dehydratase and a Delta(1)-pyrroline-2-carboxylate (Pyr2C) reductase. In order to shed light on the structure and catalysis of the enzyme involved in the second step of the T3LHyp degradation pathway, the crystal structure of Pyr2C reductase from the archaeon Thermococcus litoralis DSM 5473 complexed with NADH and L-proline is presented. The model allows the mapping of the residues involved in cofactor and product binding and represents a valid model for rationalizing the catalysis of Pyr2C reductases. | ||
- | + | Structure of Thermococcus litoralis Delta(1)-pyrroline-2-carboxylate reductase in complex with NADH and L-proline.,Ferrario E, Miggiano R, Rizzi M, Ferraris DM Acta Crystallogr D Struct Biol. 2020 May 1;76(Pt 5):496-505. doi:, 10.1107/S2059798320004866. Epub 2020 Apr 29. PMID:32355045<ref>PMID:32355045</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
- | [[Category: | + | <div class="pdbe-citations 6t3e" style="background-color:#fffaf0;"></div> |
- | [[Category: Miggiano | + | == References == |
- | [[Category: | + | <references/> |
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Thermococcus litoralis DSM 5473]] | ||
+ | [[Category: Ferrario E]] | ||
+ | [[Category: Ferraris DM]] | ||
+ | [[Category: Miggiano R]] | ||
+ | [[Category: Rizzi M]] |
Current revision
Structure of Thermococcus litoralis Delta(1)-pyrroline-2-carboxylate reductase in complex with NADH and L-proline
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