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Figure 1
The overall structure of MetB from M. ulcerans. (a) In both the PLP and the PLP and HEPES complex structures a tetramer was found similar to previous MetB structures. Each tetramer contains two functional dimers (yellow/blue, purple/green). Active sites facing out of the page are indicated in black, while active sites facing into the page are indicated in red. (b) An individual dimer of MetB contains two active sites. The main portion of the active site is made up by a pocket within the individual monomer, with a flexible loop from the second monomer closing the pocket. The PLP moiety is shown in gray. (c) The active site of MetB covalently linked to PLP. A tight hydrogen-bond network is created around the PLP moiety by residues from both of the individual monomers in the homodimer. Monomer A is indicated in blue and monomer B in yellow; hydrogen bonds are represented by black dashed lines and range from 2.4 to 3.2 Å in length. The average B factor for PLP for the MetB–PLP structure is 14.2 Å2.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
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