3PSA
Classification of a Haemophilus influenzae ABC transporter HI1470/71 through its cognate molybdate periplasmic binding protein MolA (MolA bound to tungstate)
Summary for 3PSA
| Entry DOI | 10.2210/pdb3psa/pdb |
| Related | 3PSH |
| Descriptor | protein HI_1472, TUNGSTATE(VI)ION (3 entities in total) |
| Functional Keywords | periplasmic binding protein, substrate binding protein, oxyanion binding protein, metal transport |
| Biological source | Haemophilus influenzae |
| Total number of polymer chains | 1 |
| Total formula weight | 36890.77 |
| Authors | Tirado-Lee, L.,Lee, A.,Rees, D.C.,Pinkett, H.W. (deposition date: 2010-12-01, release date: 2011-11-30, Last modification date: 2024-02-21) |
| Primary citation | Tirado-Lee, L.,Lee, A.,Rees, D.C.,Pinkett, H.W. Classification of a Haemophilus influenzae ABC Transporter HI1470/71 through Its Cognate Molybdate Periplasmic Binding Protein, MolA. Structure, 19:1701-1710, 2011 Cited by PubMed Abstract: molA (HI1472) from H. influenzae encodes a periplasmic binding protein (PBP) that delivers substrate to the ABC transporter MolB(2)C(2) (formerly HI1470/71). The structures of MolA with molybdate and tungstate in the binding pocket were solved to 1.6 and 1.7 Å resolution, respectively. The MolA-binding protein binds molybdate and tungstate, but not other oxyanions such as sulfate and phosphate, making it the first class III molybdate-binding protein structurally solved. The ∼100 μM binding affinity for tungstate and molybdate is significantly lower than observed for the class II ModA molybdate-binding proteins that have nanomolar to low micromolar affinity for molybdate. The presence of two molybdate loci in H. influenzae suggests multiple transport systems for one substrate, with molABC constituting a low-affinity molybdate locus. PubMed: 22078568DOI: 10.1016/j.str.2011.10.004 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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