|
|
| Line 1: |
Line 1: |
| [[Image:1mbt.jpg|left|200px]] | | {{Seed}} |
| | [[Image:1mbt.png|left|200px]] |
|
| |
|
| <!-- | | <!-- |
| Line 9: |
Line 10: |
| {{STRUCTURE_1mbt| PDB=1mbt | SCENE= }} | | {{STRUCTURE_1mbt| PDB=1mbt | SCENE= }} |
|
| |
|
| '''OXIDOREDUCTASE'''
| | ===OXIDOREDUCTASE=== |
|
| |
|
|
| |
|
| ==Overview==
| | <!-- |
| BACKGROUND: The repeating disaccharide and pentapeptide units of the bacterial peptidoglycan layer are connected by a lactyl ether bridge biosynthesized from UDP-N-acetylglucosamine and phosphoenolpyruvate in sequential enol ether transfer and reduction steps catalyzed by MurA and MurB respectively. Knowledge of the structure and mechanism of the MurB enzyme will permit analysis of this unusual enol ether reduction reaction and may facilitate the design of inhibitors as candidate next-generation antimicrobial agents. RESULTS: The crystal structure of UDP-N-acetylenolpyruvylglucosamine reductase, MurB, has been solved at 3.0 A and compared with our previously reported structure of MurB complexed with its substrate enolpyruvyl-UDP-N- acetylglucosamine. Comparison of the liganded structure of MurB with this unliganded form reveals that the binding of substrate induces a substantial movement of domain 3 (residues 219-319) of the enzyme and a significant rearrangement of a loop within this domain. These ligand induced changes disrupt a stacking interaction between two tyrosines (Tyr190 and Tyr254) which lie at the side of the channel leading to the active site of the free enzyme. CONCLUSIONS: The conformational change induced by enolpyruvyl-UDP-N- acetylglucosamine binding to MurB results in the closure of the substrate-binding channel over the substrate. Tyr190 swings over the channel opening and establishes a hydrogen bond with an oxygen of the alpha-phosphate of the sugar nucleotide substrate which is critical to substrate binding.
| | The line below this paragraph, {{ABSTRACT_PUBMED_8805513}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 8805513 is the PubMed ID number. |
| | --> |
| | {{ABSTRACT_PUBMED_8805513}} |
|
| |
|
| ==About this Structure== | | ==About this Structure== |
| Line 28: |
Line 32: |
| [[Category: Flavoenzyme]] | | [[Category: Flavoenzyme]] |
| [[Category: Oxidoreductase]] | | [[Category: Oxidoreductase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:52:09 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 23:38:30 2008'' |
