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Show structures: [1 - 5] [6 - 10] [11 - 15] [16 - 20] [21 - 25] [26 - 30] [31 - 35] [36 - 40] [41 - 45] [46 - 50] [51 - 55] [56 - 60] [61 - 65] [66 - 69]
An F72G mutant of the EAS hydrophobin

[ PDB file ] [ PubMed link ]

Fungi make a hydrophobic coating on their spores by assembling an amphipathic surface monolayer made from small proteins termed hydrophobins. In an effort to try to understand the structural basis for the non-covalent assembly process (in which long, thin, amyloid-like structures known as rodlets are formed), Ingrid Macindoe in Margie's lab determined the structure of a point mutant - F72G of the Neurospora hydrophobin EAS. This mutant takes much longer to form rodlets - although the rodlets that it finally forms closely resemble wildtype ones. Surprisingly the structure of F72G was indistinguishable from the wild-type protein. On the other hand, a small but measureable increase in flexibility was observed for the mutated region, suggesting that this increased dynamics is responsible for the longer lag time in rodlet formation. This work starts to give us an idea of which parts of EAS are important for rodlet formation.

And now for something completely different!

Well, this isn't the sort of structure that we are *used* to looking at here in the lab, but Paula is getting some great images of structures in murine embryos...! Now for the knockouts...

The Lhx4-Isl2 complex

[ PDB file ] [ PubMed link ]

In developing neuronal tissue expression of the key specification factor Lhx3 is supplemented by the redundant protein Lhx4. In motor neurons the balance between Lhx3 and Isl1 is critical for proper cell fate determination. In order to achieve the correct stoichiometric balance between Lhx3/4 and Isl1, Isl2 is additionally expressed to supplement Isl1 protein levels. The structure of the Lhx4 LIM domains complexed with the Isl2 LIM-interaction domain illustrates strong structural conservation in the interactions made between Lhx3/4 and Isl1/2 (when compared with our Lhx3/Isl1 structure). This emphasises the need to so strictly preserve these redundant interactions for the correct developmental outcome.

DewA - the hydrophobin from Aspergillus nidulans

[ PDB file ] [ PubMed link ]

Hydrophobins spontaneously self-assemble into functional amyloid monolayers at hydrophobic:hydrophilic interfaces. These amphipathic monolayers have amazing physicochemical properties and have been suggested for many different applications. Vanessa, under Margie's supervision, determined the st ructure of DewA. While the pattern of four disulfide bonds that is a defining feature of hydrophobins is conserved, the arrangement and composition of secondary-structure elements in DewA are quite different to what has been observed in other hydrophobin structures. Her NMR data also showed that DewA populates two conformations in solution, both of which are assembly competent. One conformer forms a dimer at high concentrations, but this dimer is off-pathway to fibril formation and may represent an assembly control mechanism. These data highlight the structural differences between fibril-forming hydrophobins and those that form amorphous monolayers.

Structure of a ZNF217-DNA complex

[ PDB file ] [ PubMed link ]

We have shown previously that a two-zinc finger unit found in the transcriptional coregulator ZNF217 recognizes DNA but with an affinity and specificity that is lower than other classical ZF arrays. To investigate the basis for these differences, we determined the structure of a ZNF217-DNA complex. We show that although the overall position of the ZFs on the DNA closely resembles that observed for other ZFs, the side-chain interaction pattern differs substantially from the canonical model. The structure also reveals the presence of two methyl-p interactions, each featuring a tyrosine contacting a thymine methyl group. To our knowledge, interactions of this type have not previously been described in classical ZF-DNA complexes. We speculate that relatively low affinity/specificity interactions of this type might be important for gene regulation.

Show structures: [1 - 5] [6 - 10] [11 - 15] [16 - 20] [21 - 25] [26 - 30] [31 - 35] [36 - 40] [41 - 45] [46 - 50] [51 - 55] [56 - 60] [61 - 65] [66 - 69]

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Lastest update: "Lab members page", on 24th Aug 2020.

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