3sma

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==A new N-acetyltransferase fold in the structure and mechanism of the phosphonate biosynthetic enzyme FrbF==
==A new N-acetyltransferase fold in the structure and mechanism of the phosphonate biosynthetic enzyme FrbF==
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<StructureSection load='3sma' size='340' side='right' caption='[[3sma]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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<StructureSection load='3sma' size='340' side='right'caption='[[3sma]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3sma]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_rubellomurinus Streptomyces rubellomurinus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SMA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SMA FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3sma]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_rubellomurinus Streptomyces rubellomurinus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SMA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SMA FirstGlance]. <br>
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</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></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&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">frbF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=359131 Streptomyces rubellomurinus])</td></tr>
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<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></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=3sma FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sma OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3sma RCSB], [http://www.ebi.ac.uk/pdbsum/3sma PDBsum]</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=3sma FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sma OCA], [https://pdbe.org/3sma PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sma RCSB], [https://www.ebi.ac.uk/pdbsum/3sma PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sma 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/Q0ZQ43_STRR3 Q0ZQ43_STRR3]
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The enzyme FrbF has attracted significant attention due to its role in The enzyme FrbF from Streptomyces rubellomurinus has attracted significant attention due to its role in the biosynthesis of the antimalarial phosphonate FR-900098. The enzyme catalyzes acetyl transfer onto the hydroxamate of the FR-900098 precursors cytidine 5'-monophosphate-3-aminopropylphosphonate and cytidine 5'-monophosphate-N-hydroxy-3-aminopropylphosphonate. In spite of the established function as a bona fide N-acetyltransferase, FrbF shows no sequence similarity with any member of the GCN5-like N-acetyltransferase (GNAT) superfamily. Here, we present the 2.0 A resolution crystal structure of FrbF in complex with acetyl-CoA that demonstrates a unique architecture that is distinct from those of canonical GNAT-like acetyltransferases. We also utilize the co-crystal structure to guide structure-function studies that identify the roles of putative active site residues in the acetyltransferase mechanism. The combined biochemical and structural analyses of FrbF provide insights into this previously uncharacterized family of N-acetyltransferases and also provides a molecular framework towards the production of novel N-acyl derivatives of FR-900098.
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A new N-acetyltransferase fold in the structure and mechanism of the phosphonate biosynthetic enzyme FrbF.,Bae B, Cobb R, Desieno MA, Zhao H, Nair SK J Biol Chem. 2011 Aug 24. PMID:21865168<ref>PMID:21865168</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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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Large Structures]]
[[Category: Streptomyces rubellomurinus]]
[[Category: Streptomyces rubellomurinus]]
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[[Category: Bae, B]]
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[[Category: Bae B]]
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[[Category: Nair, S K]]
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[[Category: Nair SK]]
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[[Category: Acetyl coa binding]]
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[[Category: N-acetyl transferase]]
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[[Category: Transferase]]
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Current revision

A new N-acetyltransferase fold in the structure and mechanism of the phosphonate biosynthetic enzyme FrbF

PDB ID 3sma

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