3fwk

<StructureSection load='3fwk' size='340' side='right' caption='[[3fwk]], [[Resolution|resolution]] 1.20&Aring;' scene=''>

<table><tr><td colspan='2'>[[3fwk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_2001 Atcc 2001]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FWK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FWK FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CAGL0K01397g, FAD1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5478 ATCC 2001])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/FAD_synthetase FAD synthetase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.2 2.7.7.2] </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=3fwk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fwk OCA], [http://pdbe.org/3fwk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3fwk RCSB], [http://www.ebi.ac.uk/pdbsum/3fwk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3fwk ProSAT]</span></td></tr>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fw/3fwk_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

Flavin mononucleotide adenylyltransferase (FMNAT) catalyzes the formation of the essential flavocoenzyme flavin adenine dinucleotide (FAD) and plays an important role in flavocoenzyme homeostasis regulation. By sequence comparison, bacterial and eukaryotic FMNAT enzymes belong to two different protein superfamilies and apparently utilize different sets of active-site residues to accomplish the same chemistry. Here we report the first structural characterization of a eukaryotic FMNAT from the pathogenic yeast Candida glabrata. Four crystal structures of C. glabrata FMNAT in different complexed forms were determined at 1.20-1.95 A resolutions, capturing the enzyme active-site states prior to and after catalysis. These structures reveal a novel flavin-binding mode and a unique enzyme-bound FAD conformation. Comparison of the bacterial and eukaryotic FMNATs provides a structural basis for understanding the convergent evolution of the same FMNAT activity from different protein ancestors. Structure-based investigation of the kinetic properties of FMNAT should offer insights into the regulatory mechanisms of FAD homeostasis by FMNAT in eukaryotic organisms.

Structure and mechanism of a eukaryotic FMN adenylyltransferase.,Huerta C, Borek D, Machius M, Grishin NV, Zhang H J Mol Biol. 2009 Jun 5;389(2):388-400. Epub 2009 Apr 16. PMID:19375431<ref>PMID:19375431</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 3fwk" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Atcc 2001]]

[[Category: FAD synthetase]]

[[Category: Borek, D]]

[[Category: Huerta, C]]

[[Category: Zhang, H]]

[[Category: Transferase]]