4KKV
Crystal structure of candida glabrata FMN adenylyltransferase D181A Mutant
Summary for 4KKV
| Entry DOI | 10.2210/pdb4kkv/pdb |
| Related | 3FWK 3G59 3G5A 3G6K |
| Descriptor | Similar to uniprot|P38913 Saccharomyces cerevisiae YDL045c FAD synthetase, beta-D-glucopyranose, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | alpha/beta protein, rossmann-like fold, transferase, fad biosynthesis |
| Biological source | Candida glabrata (Yeast) |
| Total number of polymer chains | 1 |
| Total formula weight | 36157.32 |
| Authors | Huerta, C.,Zhang, H. (deposition date: 2013-05-06, release date: 2013-05-29, Last modification date: 2023-09-20) |
| Primary citation | Huerta, C.,Grishin, N.V.,Zhang, H. The "Super Mutant" of Yeast FMN Adenylyltransferase Enhances the Enzyme Turnover Rate by Attenuating Product Inhibition. Biochemistry, 52:3615-3617, 2013 Cited by PubMed Abstract: 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. PubMed: 23663086DOI: 10.1021/bi400454w PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.74 Å) |
Structure validation
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