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Model of the polymeric EAS rodlets

[ PubMed link ]

Using our structure of the monomeric form of the hydrophobin EAS, together with a wealth of spectroscopic and other data (including X-ray fibre diffraction and mutagenesis data), we have been able to propose a couple of plausible models for the structure of the polymeric rodlets. Basically, we propose that the beta-barrels stack end to end, forming hydrogen bonds between the end strands from each barrel. The flexible loop regions may either hang off the side (top model) or form additional beta-structure that results in them being incorporated into the beta-barrel and stacking with adjacent monomers (lower model).

p22HBP - a new heme-binding protein in red blood cells

[ PDB file ] [ PubMed link ]

p22HBP is a 22-kDa mammalian protein that is highly upregulated during erythroid development, and appears to be a target gene of GATA-1. Its function is currently unknown, although it has been reported to bind to a range of different porphyrins, suggesting a role in heme biosynthesis. We have determined the structure of p22HBP and used HSQC titration data to map its porphyrin binding site. Interestingly, our structure reveals that p22HBP has structural (but not sequence) homology to a bacterial multi-drug resistance protein BmrR that functions by binding to a variety of small hydrophobic drug molecules.

HOP - a corepressor comprising a single homeodomain

[ PDB file ] [ PubMed link ]

Homeodomain-only protein (HOP) is an 8-kDa transcriptional corepressor that is essential for the normal development of the mammalian heart. A combination of sequence comparison and our structural data revealed that HOP consists entirely of a homeodomain, and it is the only human protein to have this topology. We have also shown that, unlike other classic homeodomain proteins, HOP does not appear to interact with DNA, and it appears that it instead functions as a bridge in the formation of HDAC-type repressive complexes on DNA. However, the mechanism by which this repression occurs is still only partially resolved. Our results demonstrate that the homeodomain fold has been co-opted during evolution for functions other than sequence-specific DNA binding.

The THAP domain of C. elegans CtBP

[ PDB file ] [ PubMed link ]

The THAP (Thanatos-associated protein) domain is a recently discovered zinc-binding domain found in proteins involved in transcriptional regulation, cell-cycle control, apoptosis and chromatin modification. It contains a single zinc atom ligated by cysteine and histidine residues within a Cys-X(2-4)-Cys-X(35-53)-Cys-X(2)-His consensus. We determined the NMR solution structure of the THAP domain from Caenorhabditis elegans C-terminal binding protein (CtBP) and show that it adopts a fold containing a treble clef motif, with some similarity to the zinc finger-associated domain (ZAD) from Drosophila Grauzone. We have also shown using gel-shift data that CtBP-THAP is able to bind DNA. Other THAP domains have been reported to be involved in mediating protein interactions, suggesting that THAP domains might exhibit a functional diversity similar to that observed for classical and GATA-type zinc fingers.

Structure of the fifth zinc finger of MyT1

[ PDB file ] [ PubMed link ]

MyT1 is a zinc finger transcription factor that is involved in neuronal development, controlling genes that are important for myelin sheath formation. It contains 7 zinc fingers with an unusual consensus sequence, and these domains have been shown previously to be responsible for the DNA-binding properties of MyT1. We have determined the solution structure of one of these zinc fingers, as a preliminary step towards understanding how these domains recognize DNA. The structure is different from all other known classes of zinc fingers, and contains no elements of regular secondary structure. We have gone on to examine the binding of this domain to DNA (see below!).

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

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© W. Yung 2002