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| | <StructureSection load='4zib' size='340' side='right'caption='[[4zib]], [[Resolution|resolution]] 2.05Å' scene=''> | | <StructureSection load='4zib' size='340' side='right'caption='[[4zib]], [[Resolution|resolution]] 2.05Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4zib]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Metma Metma]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZIB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZIB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4zib]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanosarcina_mazei_Go1 Methanosarcina mazei Go1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZIB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZIB FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4OG:3-(1-BENZOTHIOPHEN-3-YL)-L-ALANINE'>4OG</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.054Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pylS, MM_1445 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=192952 METMA])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4OG:3-(1-BENZOTHIOPHEN-3-YL)-L-ALANINE'>4OG</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyrrolysine--tRNA(Pyl)_ligase Pyrrolysine--tRNA(Pyl) ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.26 6.1.1.26] </span></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=4zib FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zib OCA], [https://pdbe.org/4zib PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zib RCSB], [https://www.ebi.ac.uk/pdbsum/4zib PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zib ProSAT]</span></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=4zib FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zib OCA], [http://pdbe.org/4zib PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zib RCSB], [http://www.ebi.ac.uk/pdbsum/4zib PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4zib ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PYLS_METMA PYLS_METMA]] Catalyzes the attachment of pyrrolysine to tRNA(Pyl). Pyrrolysine is a lysine derivative encoded by the termination codon UAG (By similarity). | + | [https://www.uniprot.org/uniprot/PYLS_METMA PYLS_METMA] Catalyzes the attachment of pyrrolysine to tRNA(Pyl). Pyrrolysine is a lysine derivative encoded by the termination codon UAG (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Metma]] | + | [[Category: Methanosarcina mazei Go1]] |
| - | [[Category: Guo, L T]] | + | [[Category: Guo LT]] |
| - | [[Category: Nakamura, A]] | + | [[Category: Nakamura A]] |
| - | [[Category: Soll, D]] | + | [[Category: Soll D]] |
| - | [[Category: Wang, Y S]] | + | [[Category: Wang YS]] |
| - | [[Category: Aminoacyl-trna synthetase]]
| + | |
| - | [[Category: Archaeal protein]]
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| - | [[Category: Evolution]]
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| - | [[Category: Genetic code]]
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| - | [[Category: Ligase]]
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| - | [[Category: Molecular]]
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| - | [[Category: Substrate specificity]]
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| Structural highlights
Function
PYLS_METMA Catalyzes the attachment of pyrrolysine to tRNA(Pyl). Pyrrolysine is a lysine derivative encoded by the termination codon UAG (By similarity).
Publication Abstract from PubMed
Genetically encoded non-canonical amino acids are powerful tools of protein research and engineering; in particular they allow substitution of individual chemical groups or atoms in a protein of interest. One such amino acid is the tryptophan (Trp) analog 3-benzothienyl-l-alanine (Bta) with an imino-to-sulfur substitution in the five-membered ring. Unlike Trp, Bta is not capable of forming a hydrogen bond, but preserves other properties of a Trp residue. Here we present a pyrrolysyl-tRNA synthetase-derived, engineered enzyme BtaRS that enables efficient and site-specific Bta incorporation into proteins of interest in vivo. Furthermore, we report a 2.1 A-resolution crystal structure of a BtaRS*Bta complex to show how BtaRS discriminates Bta from canonical amino acids, including Trp. To show utility in protein mutagenesis, we used BtaRS to introduce Bta to replace the Trp28 residue in the active site of Staphylococcus aureus thioredoxin. This experiment showed that not the hydrogen bond between residues Trp28 and Asp58, but the bulky aromatic side chain of Trp28 is important for active site maintenance. Collectively, our study provides a new and robust tool for checking the function of Trp in proteins.
Probing the active site tryptophan of Staphylococcus aureus thioredoxin with an analog.,Englert M, Nakamura A, Wang YS, Eiler D, Soll D, Guo LT Nucleic Acids Res. 2015 Dec 15;43(22):11061-7. doi: 10.1093/nar/gkv1255. Epub, 2015 Nov 17. PMID:26582921[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Englert M, Nakamura A, Wang YS, Eiler D, Soll D, Guo LT. Probing the active site tryptophan of Staphylococcus aureus thioredoxin with an analog. Nucleic Acids Res. 2015 Dec 15;43(22):11061-7. doi: 10.1093/nar/gkv1255. Epub, 2015 Nov 17. PMID:26582921 doi:http://dx.doi.org/10.1093/nar/gkv1255
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