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2x7b

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Crystal structure of the N-terminal acetylase Ard1 from Sulfolobus solfataricus P2

Structural highlights

2x7b is a 1 chain structure with sequence from Saccharolobus solfataricus P2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.95Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NAT_SACS2 Displays alpha (N-terminal) acetyltransferase activity. Catalyzes the covalent attachment of an acetyl moiety from acetyl-CoA to the free alpha-amino group at the N-terminus of a protein (PubMed:17511810, PubMed:23959863, PubMed:25728374). NAT is able to acetylate the alpha-amino group of methionine, alanine and serine N-terminal residue substrates, however it has a preference for Ser-N-terminal substrates (PubMed:17511810, PubMed:23959863, PubMed:25728374).^[1] ^[2] ^[3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The Scottish Structural Proteomics Facility was funded to develop a laboratory scale approach to high throughput structure determination. The effort was successful in that over 40 structures were determined. These structures and the methods harnessed to obtain them are reported here. This report reflects on the value of automation but also on the continued requirement for a high degree of scientific and technical expertise. The efficiency of the process poses challenges to the current paradigm of structural analysis and publication. In the 5 year period we published ten peer-reviewed papers reporting structural data arising from the pipeline. Nevertheless, the number of structures solved exceeded our ability to analyse and publish each new finding. By reporting the experimental details and depositing the structures we hope to maximize the impact of the project by allowing others to follow up the relevant biology.

The Scottish Structural Proteomics Facility: targets, methods and outputs.,Oke M, Carter LG, Johnson KA, Liu H, McMahon SA, Yan X, Kerou M, Weikart ND, Kadi N, Sheikh MA, Schmelz S, Dorward M, Zawadzki M, Cozens C, Falconer H, Powers H, Overton IM, van Niekerk CA, Peng X, Patel P, Garrett RA, Prangishvili D, Botting CH, Coote PJ, Dryden DT, Barton GJ, Schwarz-Linek U, Challis GL, Taylor GL, White MF, Naismith JH J Struct Funct Genomics. 2010 Jun;11(2):167-80. Epub 2010 Apr 24. PMID:20419351^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Mackay DT, Botting CH, Taylor GL, White MF. An acetylase with relaxed specificity catalyses protein N-terminal acetylation in Sulfolobus solfataricus. Mol Microbiol. 2007 Jun;64(6):1540-8. doi: 10.1111/j.1365-2958.2007.05752.x. Epub , 2007 May 18. PMID:17511810 doi:http://dx.doi.org/10.1111/j.1365-2958.2007.05752.x
↑ Liszczak G, Marmorstein R. Implications for the evolution of eukaryotic amino-terminal acetyltransferase (NAT) enzymes from the structure of an archaeal ortholog. Proc Natl Acad Sci U S A. 2013 Sep 3;110(36):14652-7. doi:, 10.1073/pnas.1310365110. Epub 2013 Aug 19. PMID:23959863 doi:http://dx.doi.org/10.1073/pnas.1310365110
↑ Chang YY, Hsu CH. Structural Basis for Substrate-specific Acetylation of Nalpha-acetyltransferase Ard1 from Sulfolobus solfataricus. Sci Rep. 2015 Mar 2;5:8673. doi: 10.1038/srep08673. PMID:25728374 doi:http://dx.doi.org/10.1038/srep08673
↑ Oke M, Carter LG, Johnson KA, Liu H, McMahon SA, Yan X, Kerou M, Weikart ND, Kadi N, Sheikh MA, Schmelz S, Dorward M, Zawadzki M, Cozens C, Falconer H, Powers H, Overton IM, van Niekerk CA, Peng X, Patel P, Garrett RA, Prangishvili D, Botting CH, Coote PJ, Dryden DT, Barton GJ, Schwarz-Linek U, Challis GL, Taylor GL, White MF, Naismith JH. The Scottish Structural Proteomics Facility: targets, methods and outputs. J Struct Funct Genomics. 2010 Jun;11(2):167-80. Epub 2010 Apr 24. PMID:20419351 doi:10.1007/s10969-010-9090-y

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2x7b"

@@ Line 3: / Line 3: @@
 <StructureSection load='2x7b' size='340' side='right'caption='[[2x7b]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2x7b]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Sulso Sulso]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X7B OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2X7B FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2x7b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus_P2 Saccharolobus solfataricus P2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X7B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X7B FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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]] 1.95&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2x7b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x7b OCA], [http://pdbe.org/2x7b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2x7b RCSB], [http://www.ebi.ac.uk/pdbsum/2x7b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2x7b ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</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=2x7b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x7b OCA], [https://pdbe.org/2x7b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x7b RCSB], [https://www.ebi.ac.uk/pdbsum/2x7b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x7b ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/NAT_SACS2 NAT_SACS2] Displays alpha (N-terminal) acetyltransferase activity. Catalyzes the covalent attachment of an acetyl moiety from acetyl-CoA to the free alpha-amino group at the N-terminus of a protein (PubMed:17511810, PubMed:23959863, PubMed:25728374). NAT is able to acetylate the alpha-amino group of methionine, alanine and serine N-terminal residue substrates, however it has a preference for Ser-N-terminal substrates (PubMed:17511810, PubMed:23959863, PubMed:25728374).<ref>PMID:17511810</ref> <ref>PMID:23959863</ref> <ref>PMID:25728374</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 31: / Line 34: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Sulso]]
+[[Category: Saccharolobus solfataricus P2]]
-[[Category: Carter, L G]]
+[[Category: Carter LG]]
-[[Category: Johnson, K A]]
+[[Category: Johnson KA]]
-[[Category: Liu, H]]
+[[Category: Liu H]]
-[[Category: Mackay, D]]
+[[Category: Mackay D]]
-[[Category: Mcmahon, S A]]
+[[Category: Mcmahon SA]]
-[[Category: Naismith, J H]]
+[[Category: Naismith JH]]
-[[Category: Oke, M]]
+[[Category: Oke M]]
-[[Category: Taylor, G L]]
+[[Category: Taylor GL]]
-[[Category: White, M F]]
+[[Category: White MF]]
-[[Category: Transferase]]

2x7b

From Proteopedia

Current revision

Crystal structure of the N-terminal acetylase Ard1 from Sulfolobus solfataricus P2

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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