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| | <StructureSection load='6kgj' size='340' side='right'caption='[[6kgj]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='6kgj' size='340' side='right'caption='[[6kgj]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6kgj]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KGJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6KGJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6kgj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KGJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KGJ FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">WDYHV1, C8orf32, NTAQ1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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]] 1.8Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein_N-terminal_glutamine_amidohydrolase Protein N-terminal glutamine amidohydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.122 3.5.1.122] </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=6kgj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kgj OCA], [https://pdbe.org/6kgj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6kgj RCSB], [https://www.ebi.ac.uk/pdbsum/6kgj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6kgj 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=6kgj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kgj OCA], [http://pdbe.org/6kgj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6kgj RCSB], [http://www.ebi.ac.uk/pdbsum/6kgj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6kgj ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/NTAQ1_HUMAN NTAQ1_HUMAN]] Mediates the side-chain deamidation of N-terminal glutamine residues to glutamate, an important step in N-end rule pathway of protein degradation. Conversion of the resulting N-terminal glutamine to glutamate renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. Does not act on substrates with internal or C-terminal glutamine and does not act on non-glutamine residues in any position. Does not deaminate acetylated N-terminal glutamine. With the exception of proline, all tested second-position residues on substrate peptides do not greatly influence the activity. In contrast, a proline at position 2, virtually abolishes deamidation of N-terminal glutamine (By similarity). | + | [https://www.uniprot.org/uniprot/NTAQ1_HUMAN NTAQ1_HUMAN] Mediates the side-chain deamidation of N-terminal glutamine residues to glutamate, an important step in N-end rule pathway of protein degradation. Conversion of the resulting N-terminal glutamine to glutamate renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. Does not act on substrates with internal or C-terminal glutamine and does not act on non-glutamine residues in any position. Does not deaminate acetylated N-terminal glutamine. With the exception of proline, all tested second-position residues on substrate peptides do not greatly influence the activity. In contrast, a proline at position 2, virtually abolishes deamidation of N-terminal glutamine (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Protein N-terminal glutamine amidohydrolase]]
| + | [[Category: Kim L]] |
| - | [[Category: Kim, L]] | + | [[Category: Kwon DH]] |
| - | [[Category: Kwon, D H]] | + | [[Category: Park MR]] |
| - | [[Category: Park, M R]] | + | [[Category: Song HK]] |
| - | [[Category: Song, H K]] | + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Ntaq1]]
| + | |
| Structural highlights
Function
NTAQ1_HUMAN Mediates the side-chain deamidation of N-terminal glutamine residues to glutamate, an important step in N-end rule pathway of protein degradation. Conversion of the resulting N-terminal glutamine to glutamate renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. Does not act on substrates with internal or C-terminal glutamine and does not act on non-glutamine residues in any position. Does not deaminate acetylated N-terminal glutamine. With the exception of proline, all tested second-position residues on substrate peptides do not greatly influence the activity. In contrast, a proline at position 2, virtually abolishes deamidation of N-terminal glutamine (By similarity).
Publication Abstract from PubMed
The N-degron pathway, formerly the N-end rule pathway, is a protein degradation process that determines the half-life of proteins based on their N-terminal residues. In contrast to the well-established in vivo studies over decades, in vitro studies of this pathway, including biochemical characterization and high-resolution structures, are relatively limited. In this study, we have developed a unique fusion technique using microtubule-associated protein 1A/1B light chain 3B, a key marker protein of autophagy, to tag the N-terminus of the proteins involved in the N-degron pathway, which enables high yield of homogeneous target proteins with variable N-terminal residues for diverse biochemical studies including enzymatic and binding assays and substrate identification. Intriguingly, crystallization showed a markedly enhanced probability, even for the N-degron complexes. To validate our results, we determined the structures of select proteins in the N-degron pathway and compared them to the PDB-deposited proteins. Furthermore, several biochemical applications of this technique were introduced. Therefore, this technique can be used as a general tool for the in vitro study of the N-degron pathway.
Use of the LC3B-fusion technique for biochemical and structural studies of proteins involved in the N-degron pathway.,Kim L, Kwon DH, Heo J, Park MR, Song HK J Biol Chem. 2020 Jan 9. pii: RA119.010912. doi: 10.1074/jbc.RA119.010912. PMID:31919097[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kim L, Kwon DH, Heo J, Park MR, Song HK. Use of the LC3B-fusion technique for biochemical and structural studies of proteins involved in the N-degron pathway. J Biol Chem. 2020 Jan 9. pii: RA119.010912. doi: 10.1074/jbc.RA119.010912. PMID:31919097 doi:http://dx.doi.org/10.1074/jbc.RA119.010912
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