7cdl | pdb_00007cdl

holo-methanol dehydrogenase (MDH) with Cys131-Cys132 reduced from Methylococcus capsulatus (Bath)

spinqualitylabelsall models 7cdl, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7cdl is a 16 chain structure with sequence from Methylococcus capsulatus str. Bath. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.85Å Ligands: CA, PQQ Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q60AR6_METCA Publication Abstract from PubMed The active site of methanol dehydrogenase (MDH) contains a rare disulfide bridge between adjacent cysteine residues. As a vicinal disulfide, the structure is highly strained, suggesting it might work together with the pyrroloquinoline quinone (PQQ) prosthetic group and the Ca(2+) ion in the catalytic turnover during methanol (CH(3)OH) oxidation. We purify MDH from Methylococcus capsulatus (Bath) with the disulfide bridge broken into two thiols. Spectroscopic and high-resolution X-ray crystallographic studies of this form of MDH indicate that the disulfide bridge is redox active. We observe an internal redox process within the holo-MDH that produces a disulfide radical anion concomitant with a companion PQQ radical, as evidenced by an optical absorption at 408 nm and a magnetically dipolar-coupled biradical in the EPR spectrum. These observations are corroborated by electron-density changes between the two cysteine sulfurs of the disulfide bridge as well as between the bound Ca(2+) ion and the O5-C5 bond of the PQQ in the high-resolution X-ray structure. On the basis of these findings, we propose a mechanism for the controlled redistribution of the two electrons during hydride transfer from the CH(3)OH in the alcohol oxidation without formation of the reduced PQQ ethenediol, a biradical mechanism that allows for possible recovery of the hydride for transfer to an external NAD(+) oxidant in the regeneration of the PQQ cofactor for multiple catalytic turnovers. In support of this mechanism, a steady-state level of the disulfide radical anion is observed during turnover of the MDH in the presence of CH(3)OH and NAD(+). Mechanism of Pyrroloquinoline Quinone-Dependent Hydride Transfer Chemistry from Spectroscopic and High-Resolution X-ray Structural Studies of the Methanol Dehydrogenase from Methylococcus capsulatus (Bath).,Chan SI, Chuankhayan P, Reddy Nareddy PK, Tsai IK, Tsai YF, Chen KH, Yu SS, Chen CJ J Am Chem Soc. 2021 Mar 10;143(9):3359-3372. doi: 10.1021/jacs.0c11414. Epub 2021 , Feb 25. PMID:33629832 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Methanol dehydrogenase

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