1h9k
TWO CRYSTAL STRUCTURES OF THE CYTOPLASMIC MOLYBDATE-BINDING PROTEIN MODG SUGGEST A NOVEL COOPERATIVE BINDING MECHANISM AND PROVIDE INSIGHTS INTO LIGAND-BINDING SPECIFICITY. PHOSPHATE-GROWN FORM WITH TUNGSTATE AND PHOSPHATE BOUND
|
OverviewOverview
The X-ray structures of the cytoplasmic molybdate-binding protein ModG, from Azotobacter vinelandii in two different crystal forms have been, determined. For such a small protein it is remarkably complex. Each 14.3, kDa subunit contains two small beta-barrel domains, which display an, OB-fold motif, also seen in the related structure of ModE, a, molybdenum-dependent transcriptional regulator, and very recently in the, Mop protein that, like ModG, has been implicated in molybdenum homeostasis, within the cell. In contrast to earlier speculation, the functional unit, of ModG is actually not a dimer (as in ModE), but a trimer capable of, binding a total of eight molybdate molecules that are distributed between, two disparate types of site. All the binding sites are located at subunit, ... [(full description)]
About this StructureAbout this Structure
1H9K is a [Single protein] structure of sequence from [Azotobacter vinelandii] with WO4 and PO4 as [ligands]. Full crystallographic information is available from [OCA].
ReferenceReference
Two crystal structures of the cytoplasmic molybdate-binding protein ModG suggest a novel cooperative binding mechanism and provide insights into ligand-binding specificity., Delarbre L, Stevenson CE, White DJ, Mitchenall LA, Pau RN, Lawson DM, J Mol Biol. 2001 May 18;308(5):1063-79. PMID:11352591
Page seeded by OCA on Mon Oct 29 21:53:38 2007