3be5 | pdb_00003be5

Crystal structure of FitE (crystal form 1), a group III periplasmic siderophore binding protein

spinqualitylabelsall models 3be5, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3be5 is a 4 chain structure with sequence from Escherichia coli o157:h7 edl933. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL NonStd Res: MSE Related: 3be6 Gene: fite, ECs3913, Z4382 (Escherichia coli O157:H7 EDL933) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Periplasmic binding proteins (PBPs) are essential components of bacterial transport systems, necessary for bacterial growth and survival. The two-domain structures of PBPs are topologically classified into three groups based on the number of crossovers or hinges between the globular domains: group I PBPs have three connections, group II have two, and group III have only one. Although a large number of structures for group I or II PBPs are known, fewer group III PBPs have been structurally characterized. Group I and II PBPs exhibit significant domain motions during transition from the unbound to ligand-bound form, however, no large conformational changes have been observed to date in group III PBPs. We have solved the crystal structure of a periplasmic binding protein FitE, part of an iron transport system, fit, recently identified in a clinical E. coli isolate. The structure, determined at 1.8 A resolution, shows that FitE is a group III PBP containing a single alpha-helix bridging the two domains. Among the individual FitE molecules present in two crystal forms we observed three different conformations (open, closed, intermediate). Our crystallographic and molecular dynamics results strongly support the notion that group III PBPs also adopt the same Venus flytrap mechanism as do groups I and II PBPs. Unlike other group III PBPs, FitE forms dimers both in solution and in the crystals. The putative siderophore binding pocket is lined with arginine residues, suggesting an anionic nature of the iron-containing siderophore. Proteins 2009. (c) 2008 Wiley-Liss, Inc. Trapping open and closed forms of FitE-A group III periplasmic binding protein.,Shi R, Proteau A, Wagner J, Cui Q, Purisima EO, Matte A, Cygler M Proteins. 2008 Sep 25;75(3):598-609. PMID:19004000 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also ABC transporter 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA