|
|
Line 1: |
Line 1: |
| [[Image:1n05.gif|left|200px]] | | {{Seed}} |
| | [[Image:1n05.png|left|200px]] |
|
| |
|
| <!-- | | <!-- |
Line 9: |
Line 10: |
| {{STRUCTURE_1n05| PDB=1n05 | SCENE= }} | | {{STRUCTURE_1n05| PDB=1n05 | SCENE= }} |
|
| |
|
| '''Crystal Structure of Schizosaccharomyces pombe Riboflavin Kinase Reveals a Novel ATP and Riboflavin Binding Fold'''
| | ===Crystal Structure of Schizosaccharomyces pombe Riboflavin Kinase Reveals a Novel ATP and Riboflavin Binding Fold=== |
|
| |
|
|
| |
|
| ==Overview==
| | <!-- |
| The essential redox cofactors riboflavin monophosphate (FMN) and flavin adenine dinucleotide (FAD) are synthesised from their precursor, riboflavin, in sequential reactions by the metal-dependent riboflavin kinase and FAD synthetase. Here, we describe the 1.6A crystal structure of the Schizosaccharomyces pombe riboflavin kinase. The enzyme represents a novel family of phosphoryl transferring enzymes. It is a monomer comprising a central beta-barrel clasped on one side by two C-terminal helices that display an L-like shape. The opposite side of the beta-barrel serves as a platform for substrate binding as demonstrated by complexes with ADP and FMN. Formation of the ATP-binding site requires significant rearrangements in a short alpha-helix as compared to the substrate free form. The diphosphate moiety of ADP is covered by the glycine-rich flap I formed from parts of this alpha-helix. In contrast, no significant changes are observed upon binding of riboflavin. The ribityl side-chain might be covered by a rather flexible flap II. The unusual metal-binding site involves, in addition to the ADP phosphates, only the strictly conserved Thr45. This may explain the preference for zinc observed in vitro. | | The line below this paragraph, {{ABSTRACT_PUBMED_12595258}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12595258 is the PubMed ID number. |
| | --> |
| | {{ABSTRACT_PUBMED_12595258}} |
|
| |
|
| ==About this Structure== | | ==About this Structure== |
Line 33: |
Line 37: |
| [[Category: Metal binding]] | | [[Category: Metal binding]] |
| [[Category: Phosphoryl transferase]] | | [[Category: Phosphoryl transferase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:55:27 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:39:08 2008'' |