4NDO
Crystal structure Molybdenum Storage Protein with fully Mo-loaded cavity
Summary for 4NDO
| Entry DOI | 10.2210/pdb4ndo/pdb |
| Related | 2OGX 4F6T 4NDP 4NDQ 4NDR |
| Descriptor | Molybdenum storage protein subunit beta, Molybdenum storage protein subunit alpha, ADENOSINE-5'-TRIPHOSPHATE, ... (9 entities in total) |
| Functional Keywords | rossmann fold, molybdenum storage, atp binding, molybdenum binding, metal binding protein |
| Biological source | Azotobacter vinelandii More |
| Total number of polymer chains | 2 |
| Total formula weight | 63830.74 |
| Authors | Poppe, J.,Warkentin, E.,Demmer, U.,Ermler, U. (deposition date: 2013-10-27, release date: 2014-08-13, Last modification date: 2023-09-20) |
| Primary citation | Poppe, J.,Warkentin, E.,Demmer, U.,Kowalewski, B.,Dierks, T.,Schneider, K.,Ermler, U. Structural diversity of polyoxomolybdate clusters along the three-fold axis of the molybdenum storage protein. J.Inorg.Biochem., 138:122-128, 2014 Cited by PubMed Abstract: The molybdenum storage protein (MoSto) can store more than 100 Mo or W atoms as discrete polyoxometalate (POM) clusters. Here, we describe the three POM cluster sites along the threefold axis of the protein complex based on four X-ray structures with slightly different polyoxomolybdate compositions between 1.35 and 2 Å resolution. In contrast to the Moα-out binding site occupied by an Mo3 cluster, the Moα-in and Moβ binding sites contain rather weak and non-uniform electron density for the Mo atoms (but clearly identifiable by anomalous data), suggesting the presence of POM cluster ensembles and/or degradation products of larger aggregates. The "Moα-in cluster ensemble" was interpreted as an antiprism-like Mo6 species superimposed with an Mo7 pyramide and the "Moβ cluster ensemble" as an Mo13 cluster (present mostly in a degraded form) composed of a pyramidal Mo7 and a Mo3 building block linked by three spatially separated MoOx units. Inside the ball-shaped Mo13 cluster sits an occluded central atom, perhaps a metal ion. POM cluster formation at the Moα-in and Moβ sites appears to be driven by filtering out and binding/protecting self-assembled transient species complementary to the protein template. PubMed: 24945101DOI: 10.1016/j.jinorgbio.2014.05.009 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.35 Å) |
Structure validation
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