EC Number   |
General Information |
Reference |
|---|
   1.14.13.25 | more |
analysis of structural and functional differences of sMMO and pMMO, EC 1.14.18.3, substrate/product/cofactor-active site interactions, docking analysis of interactions between cofactors and corresponding enzymes. Molecular simulations and modeling, overview. Structural architecture of sMMO. Enzyme sMMO requires three protein components for maximal catalytic activity: the hydroxylase (MMOH), the reductase (MMOR), and the regulatory protein (MMOB), structure-function relationships, detailed overview. MMOR consists of a NAD binding domain, an FAD-binding domain and a ferredoxin and plays a key role in the delivery of electrons within sMMO enzyme systems. The Fe2S2 domain appears to be the MMOH (methane monooxygenase hydroxylase) binding site, sMMOH docking simulations. MMOB acts as a controller of the methane-to-methanol conversion reaction |
-, 746420 |
| 1.14.13.25 | more |
enzyme sMMO contains a non-heme diiron active site, active site structure, overview. Enzyme sMMO requires three protein components for maximal catalytic activity: the hydroxylase (MMOH), the reductase (MMOR), and the regulatory protein (MMOB), detailed overview |
-, 745389 |
| 1.14.13.25 | more |
enzyme sMMO structural reorganization through subunits MMOH and MMOB including the dinuclear iron cluster, detailed overview |
764976 |
| 1.14.13.25 | more |
exogenous ligands bound to the diiron cluster of the sMMOH:MMOB complex induce conformational changes, structural analysis, overview. Bottlenecks between cavities are regulated by flexible residues. Bottleneck regulated by residues V105, F109, V285, and L289 is located between cavities 3 and 2. Cavity 2 is separated from the active site cavity 1 by another bottleneck controlled by residues L110, F188, L216, F282 and F286. Cavities 3 and 2 are connected in all of the Mt sMMOH and sMMOH:MMOB crystal structures. The MMOB binding-induced reorganization of the bottleneck residues L216 and L110 in sMMOH serves to isolate cavity 1 from cavity 2 in the complex. The pore is located between helices E and F and has been proposed to be involved in regulating the access of substrates and release of products (CH3OH) to and from the active site, respectively. The strictly conserved amino acids T213, N214, and E240 are considered the pore gating residues that regulate these processes. The pore is a uniquely polar region on the sMMOH surface as it is flanked by hydrophobic amino acids A210, V218, L237, L244, and M247 on helices E and F. The side chain of T213 lines the active site cavity and the hydroxyl moiety points towards the diiron cluster. Chemical reduction of the diiron cluster causes the middle of helix E to twist, resulting in T213 and N214 to shift 2.2 A and 3.2 A, respectively. The rotameric conformations of the hydrophobic residues V218, L244, and M247 are altered as well, helping to create a chemical environment that does not favor stable binding of water molecules to the region around the pore. MMOB binding to sMMOH causes structural rearrangement of the pore residues as well. The side chain of E240 is no longer solvent exposed, and instead, traverses the width of the Pore. This new conformation blocks the access of substrates through the Pore into the active site cavity. The side chain of T213 is shifted 2.2 A compared to its position in Mt sMMOHox and rotated about 180° compared to its position in Mt sMMOHred. This new conformation positions the side chain hydroxyl moiety of T213 to face away from the diiron cluster and form a hydrogen bond with E240. MMOB covers the pore while in complex with sMMOH, further limiting access to the active site by this route |
764175 |
| 1.14.13.25 | more |
interaction analysis of sMMO subunits and structure-function analysis, detailed overview. Alterations of hydrogen bonding or solvent accessibility occur due to the conformational changes of isoalloxazine in FAD |
-, 764425 |
| 1.14.13.25 | more |
MmoC homology modeling using structure PDB ID 1KRH.1 and the crystal structure of the monomeric MMOH-MmoB complex from Methylococcus capsulatus (PDB ID 4GAM) as a templates |
-, 764485 |
| 1.14.13.25 | more |
significant conformational changes must be imparted within sMMOH by the binding of MMOB. Small-molecule tunnel analysis, overview |
764188 |
| 1.14.13.25 | more |
soluble methane monooxygenase component interactions monitored by 19F NMR spectroscopy. Modeling for regulation in which the dynamic equilibration of MMOR and MMOB with sMMOH allows a transient formation of key reactive complexes that irreversibly pull the reaction cycle forward. The slow kinetics of exchange of the sMMOH:MMOB complex is proposed to prevent MMOR-mediated reductive quenching of the high-valent reaction cycle intermediate Q before it can react with methane |
764181 |
| 1.14.13.25 | more |
structure comparisons of the enzymes from Methylosinus sporium strain 5 and Methylosinus trichosporium strain OB3b. MMOH-MMOD complex modeling, overview |
-, 765765 |
| 1.14.13.25 | more |
structure-spectroscopy correlations for intermediate Q of soluble methane monooxygenase, QM/MM calculations. Modeling of the MMOH oxidative and reductive state, Moessbauer parameters and electronic structure of MMOHox. The selection of plausible models include the following: (1) bis-mu-oxo bridged cores, (2) mu-OepsilonGlu243 bridged diamond cores, inspired from the MMOHred structure, as suggested recently, (3) mu-oxo bridged open cores, and (4) mu-OepsilonGlu243 bridged open cores. Closed- and open-core conformations for the key intermediate in sMMO. Optimized cores of eight MOHQ models are analyzed for molecular structure and electronic structure |
764980 |
