1FR3

THE HIGH RESOLUTION STRUCTURE OF A MOLYBDATE BINDING PROTEIN FROM SPOROMUSA OVATA

Summary for 1FR3

• Entry DOI: 10.2210/pdb1fr3/pdb
• Descriptor: MOLYBDATE/TUNGSTATE BINDING PROTEIN, TUNGSTATE(VI)ION (3 entities in total)
• Functional Keywords: molybdate, tungstate, molybdate homeostasis, metal binding protein
• Biological source: Sporomusa ovata
• Total number of polymer chains: 12
• Total formula weight: 90372.39

Authors

Wagner, U.G.,Stupperich, E.,Kratky, C. (deposition date: 2000-09-07, release date: 2000-12-06, Last modification date: 2024-02-07)

Primary citation

Wagner, U.G.,Stupperich, E.,Kratky, C.
Structure of the molybdate/tungstate binding protein mop from Sporomusa ovata.
Structure Fold.Des., 8:1127-1136, 2000

PubMed Abstract: Transport of molybdenum into bacteria involves a high-affinity ABC transporter system whose expression is controlled by a repressor protein called ModE. While molybdate transport is tightly coupled to utilization in some bacteria, other organisms have molybdenum storage proteins. One class of putative molybdate storage proteins is characterized by a sequence consisting of about 70 amino acids (Mop). A tandem repeat of Mop sequences also constitutes the molybdate binding domain of ModE.

PubMed: 11080635
DOI: 10.1016/S0969-2126(00)00525-6

Experimental method

X-RAY DIFFRACTION (1.5 Å)