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| | ==The NatA (Naa10p/Naa15p) amino-terminal acetyltrasferase complex bound to AcCoA== | | ==The NatA (Naa10p/Naa15p) amino-terminal acetyltrasferase complex bound to AcCoA== |
| - | <StructureSection load='4kvo' size='340' side='right' caption='[[4kvo]], [[Resolution|resolution]] 3.15Å' scene=''> | + | <StructureSection load='4kvo' size='340' side='right'caption='[[4kvo]], [[Resolution|resolution]] 3.15Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4kvo]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Schizosaccharomyces_pombe_972h- Schizosaccharomyces pombe 972h-]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KVO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KVO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4kvo]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe_972h- Schizosaccharomyces pombe 972h-]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KVO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KVO FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 3.15Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4kvm|4kvm]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nat1, SPCC338.07c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284812 Schizosaccharomyces pombe 972h-]), ard1, SPAC15E1.08 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284812 Schizosaccharomyces pombe 972h-])</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=4kvo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kvo OCA], [https://pdbe.org/4kvo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kvo RCSB], [https://www.ebi.ac.uk/pdbsum/4kvo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kvo ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptide_alpha-N-acetyltransferase Peptide alpha-N-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.88 2.3.1.88] </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=4kvo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kvo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kvo RCSB], [http://www.ebi.ac.uk/pdbsum/4kvo PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/NAT1_SCHPO NAT1_SCHPO]] Non-catalytic component of the NatA N-terminal acetyltransferase, which catalyzes acetylation of proteins beginning with Met-Ser, Met-Gly and Met-Ala. N-acetylation plays a role in normal eukaryotic translation and processing, protect against proteolytic degradation and protein turnover. nat1 anchors ard1 and nat5 to the ribosome and may present the N termini of nascent polypeptides for acetylation (By similarity). [[http://www.uniprot.org/uniprot/ARD1_SCHPO ARD1_SCHPO]] Catalytic component of the NatA N-terminal acetyltransferase, which catalyzes acetylation of proteins beginning with Met-Ser, Met-Gly and Met-Ala. N-acetylation plays a role in normal eukaryotic translation and processing, protect against proteolytic degradation and protein turnover (By similarity). | + | [https://www.uniprot.org/uniprot/NAT1_SCHPO NAT1_SCHPO] Non-catalytic component of the NatA N-terminal acetyltransferase, which catalyzes acetylation of proteins beginning with Met-Ser, Met-Gly and Met-Ala. N-acetylation plays a role in normal eukaryotic translation and processing, protect against proteolytic degradation and protein turnover. nat1 anchors ard1 and nat5 to the ribosome and may present the N termini of nascent polypeptides for acetylation (By similarity). |
| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | N-terminal acetylation is ubiquitous among eukaryotic proteins and controls a myriad of biological processes. Of the N-terminal acetyltransferases (NATs) that facilitate this cotranslational modification, the heterodimeric NatA complex has the most diversity for substrate selection and modifies the majority of all N-terminally acetylated proteins. Here, we report the X-ray crystal structure of the 100-kDa holo-NatA complex from Schizosaccharomyces pombe, in the absence and presence of a bisubstrate peptide-CoA-conjugate inhibitor, as well as the structure of the uncomplexed Naa10p catalytic subunit. The NatA-Naa15p auxiliary subunit contains 13 tetratricopeptide motifs and adopts a ring-like topology that wraps around the NatA-Naa10p subunit, an interaction that alters the Naa10p active site for substrate-specific acetylation. These studies have implications for understanding the mechanistic details of other NAT complexes and how regulatory subunits modulate the activity of the broader family of protein acetyltransferases.
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| - | Molecular basis for N-terminal acetylation by the heterodimeric NatA complex.,Liszczak G, Goldberg JM, Foyn H, Petersson EJ, Arnesen T, Marmorstein R Nat Struct Mol Biol. 2013 Aug 4. doi: 10.1038/nsmb.2636. PMID:23912279<ref>PMID:23912279</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | == References ==
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| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Peptide alpha-N-acetyltransferase]] | + | [[Category: Large Structures]] |
| | [[Category: Schizosaccharomyces pombe 972h-]] | | [[Category: Schizosaccharomyces pombe 972h-]] |
| - | [[Category: Liszczak, G P]] | + | [[Category: Liszczak GP]] |
| - | [[Category: Marmorstein, R Q]] | + | [[Category: Marmorstein RQ]] |
| - | [[Category: Acetyltransferase]]
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| - | [[Category: Amino-terminal acetyltransferase]]
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| - | [[Category: Transferase]]
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