This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1h4i
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /> <applet load="1h4i" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h4i, resolution 1.94Å" /> '''METHYLOBACTERIUM EX...)
Next diff →
Revision as of 17:34, 29 October 2007
|
METHYLOBACTERIUM EXTORQUENS METHANOL DEHYDROGENASE
Overview
BACKGROUND: Methanol dehydrogenase (MDH) is a bacterial periplasmic, quinoprotein; it has pyrrolo-quinoline quinone (PQQ) as its prosthetic, group, requires Ca2+ for activity and uses cytochrome cL as its electron, acceptor. Low-resolution structures of MDH have already been determined., RESULTS: The structure of the alpha 2 beta 2 tetramer of MDH from, Methylobacterium extorquens has now been determined at 1.94 A with an, R-factor of 19.85%. CONCLUSIONS: The alpha-subunit of MDH has an, eight-fold radial symmetry, with its eight beta-sheets stabilized by a, novel tryptophan docking motif. The PQQ in the active site is held in, place by a coplanar tryptophan and by a novel disulphide ring formed, between adjacent cysteines which are bonded by an unusual non-planar trans, peptide bond. One ... [(full description)]
About this Structure
1H4I is a [Protein complex] structure of sequences from [Methylobacterium extorquens] with CA and PQQ as [ligands]. Active as [[1]], with EC number [1.1.99.8]. Full crystallographic information is available from [OCA].
Reference
The refined structure of the quinoprotein methanol dehydrogenase from Methylobacterium extorquens at 1.94 A., Ghosh M, Anthony C, Harlos K, Goodwin MG, Blake C, Structure. 1995 Feb 15;3(2):177-87. PMID:7735834
Page seeded by OCA on Mon Oct 29 19:38:46 2007
