The same is true for Porphyridium purpureum beta-CA and Halothiobacillus neapolitanus beta-CA. Both are composed of pseudodimers composed of two structurally homologous domains. In the case of H. neapolitanus, the domains have very little sequence homology, and one domain has lost its active site, but not the overall fold. I suspect there are many examples of this kind of multidomain chain homology that probably originates from gene duplication events.

Cheers, Roger Rowlett


Phil Jeffrey wrote:
The cadmium-utilizing marine diatom carbonic anhydrase (CA) protein has 
three consecutive CA domains that have very similar structures but 
non-identical sequences.

See:
Structure and metal exchange in the cadmium carbonic anhydrase of marine 
diatoms.
Xu Y, Feng L, Jeffrey PD, Shi Y, Morel FM.
Nature. 2008 Mar 6;452(7183):56-61.

Shankar Prasad Kanaujia wrote:
  
Dear CCP4 users,
Is there any multi-domain protein (with at least two domains) which has 
identical tertiary structure of each domain ?

Thanking you.

-regards
shankar


    

Reply via email to