Protein Science
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by CHAKRABARTI, P.
Right arrow Articles by PAL, D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by CHAKRABARTI, P.
Right arrow Articles by PAL, D.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Protein Science, Vol 6, Issue 4 851-859, Copyright © 1997 by Cold Spring Harbor Laboratory Press

ARTICLE

An electrophile-nucleophile interaction in metalloprotein structures

P. CHAKRABARTI and D. PAL
Division of Physical Chemistry, National Chemical Laboratory, Pune 411008, India

A new attractive interaction in metalloprotein structures, between the thiolate anion of a metal-bound cysteine (acting as a nucleophile) and a carbonyl carbon of a peptide group (an electrophile), has been identified. From 82 cases extracted from 23 metalloprotein structures, the interacting S and C atoms are found to be at a distance of 3.2 (+/-2) A, such that the angle S...C--O is 109{deg} (+/-15{deg}). Usually, the interacting atoms are from the same Cys residue, and to allow the S to interact with the carbonyl group the side-chain and the main-chain torsion angles deviate from those found in cysteines not bound by metals. There is a good correlation between the S...C distance and the angular deviation of the S...C vector from the normal to the peptide plane. Various data points may be envisaged to represent ``snapshots'' along the reaction coordinate for the intra-residue attack of Cys S on the CO group.
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 Protein Eng Des SelHome page
R. Bhattacharyya, D. Pal, and P. Chakrabarti
Disulfide bonds, their stereospecific environment and conservation in protein structures
Protein Eng. Des. Sel., November 1, 2004; 17(11): 795 - 808.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1997 by The Protein Society.