4kkv
From Proteopedia
(Difference between revisions)
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| - | {{STRUCTURE_4kkv| PDB=4kkv | SCENE= }} | ||
| - | ===Crystal structure of candida glabrata FMN adenylyltransferase D181A Mutant=== | ||
| - | {{ABSTRACT_PUBMED_23663086}} | ||
| - | == | + | ==Crystal structure of candida glabrata FMN adenylyltransferase D181A Mutant== |
| - | [[4kkv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Canga Canga]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KKV OCA]. | + | <StructureSection load='4kkv' size='340' side='right' caption='[[4kkv]], [[Resolution|resolution]] 1.74Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4kkv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Canga Canga]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KKV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KKV 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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3fwk|3fwk]], [[3g59|3g59]], [[3g5a|3g5a]], [[3g6k|3g6k]]</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=284593 CANGA])</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=4kkv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kkv OCA], [http://pdbe.org/4kkv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4kkv RCSB], [http://www.ebi.ac.uk/pdbsum/4kkv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4kkv ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | FMN adenylyltransferase (FMNAT) is an essential enzyme catalyzing the last step of a two-step pathway converting riboflavin (vitamin B2) to FAD, the ubiquitous flavocoenzyme. A structure-based mutagenesis and steady-state kinetic analysis of yeast FMNAT unexpectedly revealed that mutant D181A had a much faster turnover rate than the wild-type enzyme. Product inhibition analysis showed that wild-type FMNAT is strongly inhibited by FAD, whereas the D181A mutant has an attenuated product inhibition. These results provide a structural basis for the product inhibition of the enzyme and suggest that product release may be the rate-limiting step of the reaction. | ||
| - | + | The "Super Mutant" of Yeast FMN Adenylyltransferase Enhances the Enzyme Turnover Rate by Attenuating Product Inhibition.,Huerta C, Grishin NV, Zhang H Biochemistry. 2013 May 15. PMID:23663086<ref>PMID:23663086</ref> | |
| - | + | ||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4kkv" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Canga]] | [[Category: Canga]] | ||
[[Category: FAD synthetase]] | [[Category: FAD synthetase]] | ||
| - | [[Category: Huerta, C | + | [[Category: Huerta, C]] |
| - | [[Category: Zhang, H | + | [[Category: Zhang, H]] |
[[Category: Alpha/beta protein]] | [[Category: Alpha/beta protein]] | ||
[[Category: Fad biosynthesis]] | [[Category: Fad biosynthesis]] | ||
[[Category: Rossmann-like fold]] | [[Category: Rossmann-like fold]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 19:42, 5 August 2016
Crystal structure of candida glabrata FMN adenylyltransferase D181A Mutant
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