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


     

Protein Science (2004), 13:313-318. Published by Cold Spring Harbor Laboratory Press. Copyright © 2004 The Protein Society
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
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 Teeter, M. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Teeter, M. M.
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?

ACCELERATED COMMUNICATION

Myoglobin cavities provide interior ligand pathway

Martha M. Teeter

University of California at Davis, Davis, California 95616, USA Boston College, Chestnut Hill, Massachusetts 02467, USA

(RECEIVED July 26, 2003; FINAL REVISION October 22, 2003; ACCEPTED October 23, 2003)



Abstract

The myoglobin protein binds oxygen and catalyzes NO oxidation. As a key model protein, its dynamics have been well studied by spectroscopy and by crystallography as well as by simulation. Nonetheless, visualization of the mechanism of movement of ligands within myoglobin has been difficult. Coordinates of the A1 and A3 taxonomic spectral states of myoglobin from the 1 Å crystal structure (1a6g) are generated as consistent sets of correlated clusters of residues with A or B crystal alternates. Analysis of cavities in these A1 and A3 conformations clarifies the pathway of ligand motion from distal entry through interior movement to the proximal side of the heme. Cavities opened up by buried alternate conformations link the distal to the proximal side of the heme. Structural conservation highlights the relevance of this pathway to human neuroglobin. Cavity migration via myoglobin crystal alternates provides a specific link of protein structure to protein dynamics and protein function and demonstrates the relevance of substates (discrete disorder) to function for all proteins.

Keywords: Protein dynamics; substates; ligand migration in myoglobin; protein function

Abbreviations: psec, picosecond • nsec, nanosecond

Reprint requests to: Martha M. Teeter, University of California at Davis, Davis, Department of Chemistry, 1 Shields Avenue, Davis, CA 95616, USA; e-mail: teeter{at}ucdavis.edu; fax: (530) 752-8995.

Article and publication are at http://www.proteinscience.org/cgi/doi/10.1110/ps.03334304.


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
 Proc. Natl. Acad. Sci. USAHome page
J. Z. Ruscio, D. Kumar, M. Shukla, M. G. Prisant, T. M. Murali, and A. V. Onufriev
Atomic level computational identification of ligand migration pathways between solvent and binding site in myoglobin
PNAS, July 8, 2008; 105(27): 9204 - 9209.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
H. Ishikawa, K. Kwak, J. K. Chung, S. Kim, and M. D. Fayer
Direct observation of fast protein conformational switching
PNAS, June 24, 2008; 105(25): 8619 - 8624.
[Abstract] [Full Text] [PDF]

Home page
 Protein Sci.Home page
L. Mouawad, C. Tetreau, S. Abdel-Azeim, D. Perahia, and D. Lavalette
CO migration pathways in cytochrome P450cam studied by molecular dynamics simulations
Protein Sci., May 1, 2007; 16(5): 781 - 794.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
D. Dantsker, C. Roche, U. Samuni, G. Blouin, J. S. Olson, and J. M. Friedman
The Position 68(E11) Side Chain in Myoglobin Regulates Ligand Capture, Bond Formation with Heme Iron, and Internal Movement into the Xenon Cavities
J. Biol. Chem., November 18, 2005; 280(46): 38740 - 38755.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
D. Hamdane, L. Kiger, G. H. B. Hoa, S. Dewilde, J. Uzan, T. Burmester, T. Hankeln, L. Moens, and M. C. Marden
High Pressure Enhances Hexacoordination in Neuroglobin and Other Globins
J. Biol. Chem., November 4, 2005; 280(44): 36809 - 36814.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
D. de Sanctis, S. Dewilde, C. Vonrhein, A. Pesce, L. Moens, P. Ascenzi, T. Hankeln, T. Burmester, M. Ponassi, M. Nardini, et al.
Bishistidyl Heme Hexacoordination, a Key Structural Property in Drosophila melanogaster Hemoglobin
J. Biol. Chem., July 22, 2005; 280(29): 27222 - 27229.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
P. W. Fenimore, H. Frauenfelder, B. H. McMahon, and R. D. Young
Bulk-solvent and hydration-shell fluctuations, similar to {alpha}- and {beta}-fluctuations in glasses, control protein motions and functions
PNAS, October 5, 2004; 101(40): 14408 - 14413.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2004 by The Protein Society.