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The atomic resolution structure of methanol dehydrogenase from Methylobacterium extorquens

The atomic resolution structure of methanol dehydrogenase from Methylobacterium extorquens
The atomic resolution structure of methanol dehydrogenase from Methylobacterium extorquens
The crystal structure of methanol dehydrogenase (MDH) from Methylobacterium extorquens has been refined without stereochemical restraints at a resolution of 1.2 Å. The high-resolution data have defined the conformation of the tricyclic pyrroloquinoline quinone (PQQ) cofactor ring as entirely planar. The detailed definition of the active-site geometry has shown many features that are similar to the quinohaemoprotein alcohol dehydrogenases from Comamonas testosteroni and Pseudomonas putida, both of which possess MDH-like and cytochrome c-like domains. Conserved features between the two types of PQQ-containing enzyme suggest a common pathway for electron transfer between MDH and its physiological electron acceptor cytochrome cL. A pathway for proton transfer from the active site to the bulk solvent is also suggested.
methanol dehydrogenase, 1w6s, r1w6ssf
0907-4449
75-79
Williams, P.A.
18f55b81-ad5c-4db1-892a-9bdcc5092a6b
Coates, L.
2be36c11-8cb2-4518-a001-953051aa6a23
Mohammed, F.
e6dd5a98-bea5-484a-873a-da499c034594
Gill, R.
95656ecb-604f-425e-ac66-7dd36e47d94d
Erskine, P.T.
c77b60c5-b80c-4e6a-a103-bf57ecfcbcf6
Coker, A.
c64a7d9b-3a0d-4e79-a3eb-aaa64920116a
Wood, S.P.
430faabf-7f5c-4cf6-9bcc-5955f5e09566
Anthony, C.
6851d062-3caf-43dd-8e10-06dd25684146
Cooper, J.B.
d9f0f6a8-1260-48fc-aa5c-3dbc650e3ec0
Williams, P.A.
18f55b81-ad5c-4db1-892a-9bdcc5092a6b
Coates, L.
2be36c11-8cb2-4518-a001-953051aa6a23
Mohammed, F.
e6dd5a98-bea5-484a-873a-da499c034594
Gill, R.
95656ecb-604f-425e-ac66-7dd36e47d94d
Erskine, P.T.
c77b60c5-b80c-4e6a-a103-bf57ecfcbcf6
Coker, A.
c64a7d9b-3a0d-4e79-a3eb-aaa64920116a
Wood, S.P.
430faabf-7f5c-4cf6-9bcc-5955f5e09566
Anthony, C.
6851d062-3caf-43dd-8e10-06dd25684146
Cooper, J.B.
d9f0f6a8-1260-48fc-aa5c-3dbc650e3ec0

Williams, P.A., Coates, L., Mohammed, F., Gill, R., Erskine, P.T., Coker, A., Wood, S.P., Anthony, C. and Cooper, J.B. (2005) The atomic resolution structure of methanol dehydrogenase from Methylobacterium extorquens. Acta Crystallographica Section D: Biological Crystallography, 61 (1), 75-79. (doi:10.1107/S0907444904026964).

Record type: Article

Abstract

The crystal structure of methanol dehydrogenase (MDH) from Methylobacterium extorquens has been refined without stereochemical restraints at a resolution of 1.2 Å. The high-resolution data have defined the conformation of the tricyclic pyrroloquinoline quinone (PQQ) cofactor ring as entirely planar. The detailed definition of the active-site geometry has shown many features that are similar to the quinohaemoprotein alcohol dehydrogenases from Comamonas testosteroni and Pseudomonas putida, both of which possess MDH-like and cytochrome c-like domains. Conserved features between the two types of PQQ-containing enzyme suggest a common pathway for electron transfer between MDH and its physiological electron acceptor cytochrome cL. A pathway for proton transfer from the active site to the bulk solvent is also suggested.

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Published date: 2005
Keywords: methanol dehydrogenase, 1w6s, r1w6ssf
Organisations: Biological Sciences

Identifiers

Local EPrints ID: 24090
URI: https://eprints.soton.ac.uk/id/eprint/24090
ISSN: 0907-4449
PURE UUID: 1659f77b-d16b-4cc6-9b72-fc56ca4f240a

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Date deposited: 22 Mar 2006
Last modified: 17 Jul 2017 16:15

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Contributors

Author: P.A. Williams
Author: L. Coates
Author: F. Mohammed
Author: R. Gill
Author: P.T. Erskine
Author: A. Coker
Author: S.P. Wood
Author: C. Anthony
Author: J.B. Cooper

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