The structure of the ice binding protein Maxi from Peter Davies lab (Sun et al. 
2014, Science 343, 795-798) had a whole network of pentagonal waters that were 
critical in holding its unusual structure (waters in the core) together.

------
Arun Malhotra
Associate Professor of Biochemistry & Molecular Biology
Director, Master's in Biomedical Sciences (MiBS)

University of Miami Miller School of Medicine         Phone: (305) 243-2826
PO Box 016129                                                          Lab:   
(305) 243-2890
Miami, FL 33101                                           E-Mail: 
amalho...@miami.edu <mailto:amalho...@miami.edu>

> On Sep 27, 2019, at 7:33 AM, Vijaykumar Pillalamarri 
> <vijaypkuma...@gmail.com> wrote:
> 
> Dear Community,
> 
> I solved the structure of a protein from vibrio. There are two molecules in 
> the asymmetric unit of this protein. At the dimer interface, the C-termini of 
> both the chains interact with each other with the help of five water 
> molecules that form a pentagon. I have attached an image showing both the 
> chains and stereo image of dimer interface in the inset. I was wondering if 
> there is any significance to this or if there is any relevant literature that 
> explains this behavior.
> 
> Thank you
> Vijaykumar Pillalamarri
> C/O: Dr. Anthony Addlagatta
> Principal Scientist
> CSIR-IICT, Tarnaka
> Hyderabad, India-500007
> Mobile: +918886922975
> 
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