2J55

X-ray reduced Paraccocus denitrificans methylamine dehydrogenase O- quinone in complex with amicyanin.

Summary for 2J55

• Entry DOI: 10.2210/pdb2j55/pdb
• Related: 1AAC 1AAJ 1AAN 1BXA 1MDA 1MG2 1MG3 1SF3 1SF5 1SFD 1SFH 1T5K 2BBK 2J56 2J57 2MTA 2RAC
• Descriptor: AMICYANIN, METHYLAMINE DEHYDROGENASE HEAVY CHAIN, METHYLAMINE DEHYDROGENASE LIGHT CHAIN, ... (6 entities in total)
• Functional Keywords: oxidoreductase, transport, periplasmic, metal-binding, electron transport, single crystal microspectrophotometry
• Biological source: PARACOCCUS DENITRIFICANS; More
• Cellular location: Periplasm: P22364 P29894 P22619
• Total number of polymer chains: 6
• Total formula weight: 136825.76

Authors

Pearson, A.R.,Pahl, R.,Davidson, V.L.,Wilmot, C.M. (deposition date: 2006-09-12, release date: 2007-01-23, Last modification date: 2024-05-01)

Primary citation

Pearson, A.R.,Pahl, R.,Kovaleva, E.G.,Davidson, V.L.,Wilmot, C.M.
Tracking X-Ray-Derived Redox Changes in Crystals of a Methylamine Dehydrogenase/Amicyanin Complex Using Single-Crystal Uv/Vis Microspectrophotometry.
J.Synchrotron Radiat., 14:92-, 2007

PubMed Abstract: X-ray exposure during crystallographic data collection can result in unintended redox changes in proteins containing functionally important redox centers. In order to directly monitor X-ray-derived redox changes in trapped oxidative half-reaction intermediates of Paracoccus denitrificans methylamine dehydrogenase, a commercially available single-crystal UV/Vis microspectrophotometer was installed on-line at the BioCARS beamline 14-BM-C at the Advanced Photon Source, Argonne, USA. Monitoring the redox state of the intermediates during X-ray exposure permitted the creation of a general multi-crystal data collection strategy to generate true structures of each redox intermediate.

PubMed: 17211075
DOI: 10.1107/S0909049506051259

Experimental method

X-RAY DIFFRACTION (2.15 Å)