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Recent news

24 Aug, 2015: Ana's lab baby update...

19 Aug, 2015: Welcome to new lab members - Mehdi, Jason (aka. Alex) and Taylor

19 Aug, 2015: GATA1-DNA structure published



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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 - 64]
RbAp48 bound to MTA1(670-711)

[ PDB file ] [ PubMed link ]

A *third* structure of the RbAp48-MTA1 subcomplex - just for good measure. No extra interactions this time though...

The surprise PR domain of FOG1

[ PDB file ] [ PubMed link ]

Many years ago, Gerd and I spotted a section of FOG1 outside the ZFs that looked like it might have been ordered. After only 12 years or so, Joel finally finished solving the structure of the domain (which is only ~110 residues, so who knows *why* it took him so long!). It turns out to be a PR domain - a fold that is essentially the same as the SET domains that act as methyltransferases - mostly adding methyl groups tolysines at the N-terminal tails of histones. This means that FOG1 is *potentially* an enzyme, although we were unable to demonstrate methyltransferase activity (via a collaboration with Masoud Vedadi in Toronto). It also makes FOG1 a member of a family of 16 other human proteins that contain this domain - some of which *have* been demonstrated to be enzymes. So, we shall see...

The double ZF of GATA1 bound to pseudopalindromic DNA

[ PDB file ] [ PubMed link ]

Nina Ripin, a German Masters student, was able to determine this structure with help from David Jacques and Mitchell Guss. analysis of the structure indicates that although the N-terminal ZF (NF) can modulate GATA1 DNA binding, the NF binds DNA so poorly under physiological conditionsthat it cannot play a direct role in DNA looping (a suggestion made recently). Rather, the ability of the NF to stabilise transcriptional complexes through protein-protein interactions, and thereby recruit looping factors such as Ldb1, seems a more likely model for GATA-mediated looping.

The haloalkane dehydrogenase DmrA

[ PDB file ] [ PubMed link ]

Haloalkane dehalogenases (HLDs) catalyse the hydrolysis of haloalkanes to alcohols, offering a biological solution for toxic haloalkane industrial wastes. Hundreds of putative HLD genes have been identified in bacterial genomes, but relatively few enzymes have been characterised. We identified two novel HLDs in the genome of Mycobacterium rhodesiae strain JS60, an isolate from an organochlorine-contaminated site: DmrA and DmrB. Both recombinant enzymes were active against C2-C6 haloalkanes, with a preference for brominated linear substrates. However, DmrA had higher activity against a wider range of substrates, such as 4-bromobutyronitrile. We determined the crystal structure of selenomethionyl DmrA to 1.7 Å resolution. A spacious active site and alternate conformations of a methionine side-chain in the slot access tunnel may contribute to the broad substrate activity of DmrA. M. rhodesiae JS60 can utilise 1-iodopropane, 1-iodobutane and 1-bromobutane as sole carbon and energy sources, and this ability appears to be conferred predominantly through DmrA, which shows significantly higher levels of upregulation in response to haloalkanes than DmrB.

Now we have crystallographers solving NMR structures!

Stay tuned for more information...

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 - 64]

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Lastest update: "Lab members page", on 25th Aug 2015.


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