3CNI
Crystal structure of a domain of a putative ABC type-2 transporter from Thermotoga maritima MSB8
Summary for 3CNI
Entry DOI | 10.2210/pdb3cni/pdb |
Descriptor | Putative ABC type-2 transporter, CALCIUM ION (3 entities in total) |
Functional Keywords | structural genomics, abc type-2 transporter, thermotoga maritima, psi-2, protein structure initiative, midwest center for structural genomics, mcsg, transport protein |
Biological source | Thermotoga maritima MSB8 |
Total number of polymer chains | 1 |
Total formula weight | 17217.44 |
Authors | Filippova, E.V.,Shumilin, I.,Tkaczuk, K.L.,Cymborowski, M.,Chruszcz, M.,Xu, X.,Que, Q.,Savchenko, A.,Edwards, A.M.,Joachimiak, A.,Minor, W.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2008-03-25, release date: 2008-04-08, Last modification date: 2022-04-13) |
Primary citation | Filippova, E.V.,Tkaczuk, K.L.,Chruszcz, M.,Xu, X.,Savchenko, A.,Edwards, A.,Minor, W. Structural characterization of the putative ABC-type 2 transporter from Thermotoga maritima MSB8. J.Struct.Funct.Genom., 15:215-222, 2014 Cited by PubMed Abstract: This study describes the structure of the putative ABC-type 2 transporter TM0543 from Thermotoga maritima MSB8 determined at a resolution of 2.3 Å. In comparative sequence-clustering analysis, TM0543 displays similarity to NatAB-like proteins, which are components of the ABC-type Na(+) efflux pump permease. However, the overall structure fold of the predicted nucleotide-binding domain reveals that it is different from any known structure of ABC-type efflux transporters solved to date. The structure of the putative TM0543 domain also exhibits different dimer architecture and topology of its presumed ATP binding pocket, which may indicate that it does not bind nucleotide at all. Structural analysis of calcium ion binding sites found at the interface between TM0543 dimer subunits suggests that protein may be involved in ion-transporting activity. A detailed analysis of the protein sequence and structure is presented and discussed. PubMed: 25306867DOI: 10.1007/s10969-014-9189-7 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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