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 DENESSIOUK, K. A.
Right arrow Articles by JOHNSON, M. S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by DENESSIOUK, K. A.
Right arrow Articles by JOHNSON, M. S.
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 7, Issue 5 1136-1146, Copyright © 1998 by Cold Spring Harbor Laboratory Press

ARTICLE

Two ``unrelated'' families of ATP-dependent enzymes share extensive structural similarities about their cofactor binding sites

K. A. DENESSIOUK, J. V. LEHTONEN, T. KORPELA and M. S. JOHNSON
Joint Biotechnology Laboratory, Department of Biochemistry, University of Turku, BioCity 6A, FIN-20520 Turku, Finland Moscow Institute of Physics and Technology, 141700, Dolgoprudny, Russia Current address: Department of Biochemistry and Pharmacy, Abo Akademi University, BioCity 3A, FIN-20521 Turku, Finland.

Two proteins, D-alanine:D-alanine ligase and cAMP-dependent protein kinase, share a remarkable degree of structural convergence despite having different three-dimensional folds and different enzymatic functions. Here we report that as many as 103 residues from 10 segments form two identical super-secondary structures between which the cofactor ATP is bound. The cofactor, two bound metal cations, and several water molecules form a large network of electrostatic and hydrophobic interactions common to both enzymes, and these are mediated by the similar placement of equivalent amino acids within the common supersecondary structures.
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
 Nucleic Acids ResHome page
S. Balaji and L. Aravind
The RAGNYA fold: a novel fold with multiple topological variants found in functionally diverse nucleic acid, nucleotide and peptide-binding proteins
Nucleic Acids Res., September 27, 2007; 35(17): 5658 - 5671.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
A. Stark and R. B. Russell
Annotation in three dimensions. PINTS: Patterns in Non-homologous Tertiary Structures
Nucleic Acids Res., July 1, 2003; 31(13): 3341 - 3344.
[Abstract] [Full Text] [PDF]

Home page
 Protein Sci.Home page
Y. Gholizadeh, M. Prevost, F. Van Bambeke, B. Casadewall, P.M. Tulkens, and P. Courvalin
Sequencing of the ddl gene and modeling of the mutated D-alanine:D-alanine ligase in glycopeptide-dependent strains of Enterococcus faecium
Protein Sci., April 1, 2001; 10(4): 836 - 844.
[Abstract] [Full Text]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1998 by The Protein Society.