5k9n

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==Structural and Mechanistic Analysis of Drosophila melanogaster Polyamine N acetyltransferase, an enzyme that Catalyzes the Formation of N acetylagmatine==
==Structural and Mechanistic Analysis of Drosophila melanogaster Polyamine N acetyltransferase, an enzyme that Catalyzes the Formation of N acetylagmatine==
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<StructureSection load='5k9n' size='340' side='right' caption='[[5k9n]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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<StructureSection load='5k9n' size='340' side='right'caption='[[5k9n]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5k9n]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K9N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K9N FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5k9n]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K9N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5K9N FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CG15766, Dmel_CG15766 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<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=5k9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k9n OCA], [http://pdbe.org/5k9n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k9n RCSB], [http://www.ebi.ac.uk/pdbsum/5k9n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k9n ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5k9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k9n OCA], [https://pdbe.org/5k9n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5k9n RCSB], [https://www.ebi.ac.uk/pdbsum/5k9n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5k9n ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q9W469_DROME Q9W469_DROME]
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Agmatine N-acetyltransferase (AgmNAT) catalyzes the formation of N-acetylagmatine from acetyl-CoA and agmatine. Herein, we provide evidence that Drosophila melanogaster AgmNAT (CG15766) catalyzes the formation of N-acetylagmatine using an ordered sequential mechanism; acetyl-CoA binds prior to agmatine to generate an AgmNAT*acetyl-CoA*agmatine ternary complex prior to catalysis. Additionally, we solved a crystal structure for the apo form of AgmNAT with an atomic resolution of 2.3 A, which points towards specific amino acids that may function in catalysis or active site formation. Using the crystal structure, primary sequence alignment, pH-activity profiles, and site-directed mutagenesis, we evaluated a series of active site amino acids in order to assign their functional roles in AgmNAT. More specifically, pH-activity profiles identified at least one catalytically important, ionizable group with an apparent pKa of ~7.5, which corresponds to the general base in catalysis, Glu-34. Moreover, these data led to a proposed chemical mechanism, which is consistent with the structure and our biochemical analysis of AgmNAT.
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Structural and Mechanistic Analysis of Drosophila melanogaster Agmatine N-Acetyltransferase, an Enzyme that Catalyzes the Formation of N-Acetylagmatine.,Dempsey DR, Nichols DA, Battistini MR, Pemberton O, Ospina SR, Zhang X, Carpenter AM, O'Flynn BG, Leahy JW, Kanwar A, Lewandowski EM, Chen Y, Merkler DJ Sci Rep. 2017 Oct 18;7(1):13432. doi: 10.1038/s41598-017-13669-6. PMID:29044148<ref>PMID:29044148</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5k9n" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Drome]]
 
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[[Category: Battistini, M R]]
 
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[[Category: Carpenter, A M]]
 
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[[Category: Chen, Y]]
 
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[[Category: Dempsey, D R]]
 
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[[Category: Merkler, D J]]
 
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[[Category: Nichols, D A]]
 
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[[Category: Ospina, S R]]
 
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[[Category: Pemberton, O]]
 
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[[Category: Zhang, X]]
 
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[[Category: Acetyl-coa]]
 
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[[Category: Agmatine]]
 
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[[Category: And protein crystallography]]
 
[[Category: Drosophila melanogaster]]
[[Category: Drosophila melanogaster]]
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[[Category: Enzyme mechanism]]
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[[Category: Large Structures]]
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[[Category: N acetylagmatine]]
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[[Category: Battistini MR]]
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[[Category: Polyamine n acetyltransferase]]
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[[Category: Carpenter A-M]]
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[[Category: Transferase]]
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[[Category: Chen Y]]
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[[Category: Dempsey DR]]
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[[Category: Merkler DJ]]
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[[Category: Nichols DA]]
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[[Category: Ospina SR]]
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[[Category: Pemberton O]]
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[[Category: Zhang X]]

Current revision

Structural and Mechanistic Analysis of Drosophila melanogaster Polyamine N acetyltransferase, an enzyme that Catalyzes the Formation of N acetylagmatine

PDB ID 5k9n

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