Re: [ccp4bb] minor off topic protein symmetry

2024-06-29 Thread Artem Evdokimov
It is possible that the following tetramer displays the features you seek:

https://www.rcsb.org/structure/6v1v

You will notice that this is P1. When I solved it, I had at first some
trouble recognizing why this molecule does not have a P4 (I am slow, I
guess) but then it dawned on me :) It displays one of the cutest symmetry
transitions that I've seen so far.

Artem

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On Thu, Jun 27, 2024 at 8:46 AM Andrew Lovering 
wrote:

> Dear wise list,
>
>
>
> I have a question regarding protein oligomers that have multiple,
> differing axes of symmetry – stimulated by some perplexing but likely real
> Alphafold models.
>
>
>
> I think it’s the protein equivalent of this old chestnut:
> https://en.wikipedia.org/wiki/Three_utilities_problem
>
>
>
> Consider a trimeric fibre (perhaps collagen a good starting example) – it
> can have global 3-fold symmetry, and if it breaks from this, it is then
> able to “re-obey” this symmetry later on, but that axis is approximately
> the same as the starting one. I.e. a long winding rope with a kink in the
> middle, and the protein doesn’t have to do much to accommodate this.
>
>
>
> What happens when a long protein has multiple, dissimilar axes of
> symmetry? I.e. perhaps a trimer with the start and end on the same axis,
> but the middle domain sits ~90 degrees to this (and is also a 3-fold
> arrangement of chains A,B & C). I think I’d be correct in assuming that all
> 3 chains cannot have the same conformation – is this true?
>
> I’d argue that the protein has to unwind a little at the junctions and
> each chain takes a different path in space when migrating from axis 1> axis
> 2> back to axis 1? (think of 1 as up/down, 2 as left/right). This is
> because as each chain leaves the centre of mass of axis 1, it is a
> different distance away from the centre of mass of axis 2….?
>
>
>
> I hope that makes some sense!
>
>
>
> So my question is, does anyone have an example PDB that does something
> similar, and were they able to trace the different chains, demonstrating
> the different conformations.
>
>
>
> Thanks in advance - Andy
>
> --
>
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[ccp4bb] minor off topic protein symmetry

2024-06-27 Thread Andrew Lovering
Dear wise list,

I have a question regarding protein oligomers that have multiple, differing 
axes of symmetry - stimulated by some perplexing but likely real Alphafold 
models.

I think it's the protein equivalent of this old chestnut: 
https://en.wikipedia.org/wiki/Three_utilities_problem

Consider a trimeric fibre (perhaps collagen a good starting example) - it can 
have global 3-fold symmetry, and if it breaks from this, it is then able to 
"re-obey" this symmetry later on, but that axis is approximately the same as 
the starting one. I.e. a long winding rope with a kink in the middle, and the 
protein doesn't have to do much to accommodate this.

What happens when a long protein has multiple, dissimilar axes of symmetry? 
I.e. perhaps a trimer with the start and end on the same axis, but the middle 
domain sits ~90 degrees to this (and is also a 3-fold arrangement of chains A,B 
& C). I think I'd be correct in assuming that all 3 chains cannot have the same 
conformation - is this true?
I'd argue that the protein has to unwind a little at the junctions and each 
chain takes a different path in space when migrating from axis 1> axis 2> back 
to axis 1? (think of 1 as up/down, 2 as left/right). This is because as each 
chain leaves the centre of mass of axis 1, it is a different distance away from 
the centre of mass of axis 2?

I hope that makes some sense!

So my question is, does anyone have an example PDB that does something similar, 
and were they able to trace the different chains, demonstrating the different 
conformations.

Thanks in advance - Andy



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