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| | <StructureSection load='5k18' size='340' side='right'caption='[[5k18]], [[Resolution|resolution]] 2.73Å' scene=''> | | <StructureSection load='5k18' size='340' side='right'caption='[[5k18]], [[Resolution|resolution]] 2.73Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5k18]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Canaw Canaw]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K18 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K18 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5k18]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_albicans_WO-1 Candida albicans WO-1] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K18 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5K18 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</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]] 2.73Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5k04|5k04]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CAWG_01335 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=294748 CANAW]), CAWG_00748 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=294748 CANAW])</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=5k18 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k18 OCA], [https://pdbe.org/5k18 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5k18 RCSB], [https://www.ebi.ac.uk/pdbsum/5k18 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5k18 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=5k18 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k18 OCA], [http://pdbe.org/5k18 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k18 RCSB], [http://www.ebi.ac.uk/pdbsum/5k18 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k18 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/C4YFL7_CANAW C4YFL7_CANAW] |
| | <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: Canaw]] | + | [[Category: Candida albicans WO-1]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Cai, Y]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Han, A]] | + | [[Category: Cai Y]] |
| - | [[Category: Hong, H]] | + | [[Category: Han A]] |
| - | [[Category: Zhang, S]] | + | [[Category: Hong H]] |
| - | [[Category: N-terminal acetyltransferase complex]]
| + | [[Category: Zhang S]] |
| - | [[Category: Transferase-transferase inhibitor complex]]
| + | |
| Structural highlights
Function
C4YFL7_CANAW
Publication Abstract from PubMed
The NatB N-terminal acetyltransferase specifically acetylates the N-terminal group of substrate protein peptides starting with Met-Asp/Glu/Asn/Gln. How NatB recognizes and acetylates these substrates remains unknown. Here, we report crystal structures of a NatB holoenzyme from Candida albicans in the presence of its co-factor CoA and substrate peptides. The auxiliary subunit Naa25 of NatB forms a horseshoe-like deck to hold specifically its catalytic subunit Naa20. The first two amino acids Met and Asp of a substrate peptide mediate the major interactions with the active site in the Naa20 subunit. The hydrogen bonds between the substrate Asp and pocket residues of Naa20 are essential to determine the NatB substrate specificity. Moreover, a hydrogen bond between the amino group of the substrate Met and a carbonyl group in the Naa20 active site directly anchors the substrate toward acetyl-CoA. Together, these structures define a unique molecular mechanism of specific N-terminal acetylation acted by NatB.
Molecular Basis of Substrate Specific Acetylation by N-Terminal Acetyltransferase NatB.,Hong H, Cai Y, Zhang S, Ding H, Wang H, Han A Structure. 2017 Apr 4;25(4):641-649.e3. doi: 10.1016/j.str.2017.03.003. PMID:28380339[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hong H, Cai Y, Zhang S, Ding H, Wang H, Han A. Molecular Basis of Substrate Specific Acetylation by N-Terminal Acetyltransferase NatB. Structure. 2017 Apr 4;25(4):641-649.e3. doi: 10.1016/j.str.2017.03.003. PMID:28380339 doi:http://dx.doi.org/10.1016/j.str.2017.03.003
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