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


     

Published online before print May 28, 2004, 10.1110/ps.03571004
Protein Science (2004), 13:1724-1734. 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 All Versions of this Article:
ps.03571004v1
13/7/1724    most recent
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 Bottoms, C. A.
Right arrow Articles by Tanner, J. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bottoms, C. A.
Right arrow Articles by Tanner, J. J.
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?

Crystal structure of rat {alpha}-parvalbumin at 1.05 Å resolution

Christopher A. Bottoms1, Jonathan P. Schuermann1, Sayeh Agah2, Michael T. Henzl2 and John J. Tanner1,2

1 Department of Chemistry and
2 Department of Biochemistry, University of Missouri–Columbia, Columbia, Missouri 65211, USA

(RECEIVED December 18, 2003; FINAL REVISION April 1, 2004; ACCEPTED April 1, 2004)



Abstract

The crystal structure of rat {alpha}-parvalbumin has been determined at 1.05 Å resolution, using synchrotron data collected at Advanced Photon Source beamline 19-ID. After refinement with SHELX, employing anisotropic displacement parameters and riding hydrogen atoms, R = 0.132 and Rfree = 0.162. The average coordinate estimated standard deviations are 0.021 Å and 0.038 Å for backbone atoms and side-chain atoms, respectively. Besides providing a more precise view of the {alpha}-isoform than previously available, these data permit comparison with the 0.91 Å structure determined for pike {beta}-parvalbumin. Visualization of the anisotropic displacement parameters as thermal ellipsoids yields insight into the atomic motion within the Ca2+-binding sites. The asymmetric unit includes three parvalbumin (PV) molecules. Interestingly, the EF site in one displays uncharacteristic flexibility. The ellipsoids for Asp-92 are particularly large and non-spherical, and the shape of the Ca2+ ellipsoid implies significant vibrational motion perpendicular to the plane defined by the four y and z ligands. The relative dearth of crystal-packing interactions in this site suggests that the heightened flexibility may be the result of diminished intermolecular contacts. The implication is that, by impeding conformational mobility, crystal-packing forces may cause serious overestimation of EF-hand rigidity. The high quality of the data permitted 11 residues to be modeled in alternative side-chain conformations, including the two core residues, Ile-97 and Leu-105. The discrete disorder observed for Ile-97 may have functional ramifications, providing a mechanism for communicating binding status between the CD and EF binding loops and between the PV metal ion-binding domain and the N-terminal AB region.

Keywords: parvalbumin; EF-hand; Ca2+-binding proteins; atomic resolution crystallography

Abbreviations: PV, parvalbumin • RMSD, root-mean-square difference • e.s.d., estimated standard deviation • PDB, Protein Data Bank • ADP, anisotropic displacement parameter

Reprint requests to: John J. Tanner, Department of Chemistry, University of Missouri–Columbia, Columbia, MO 65211, USA; e-mail: tannerjj{at}missouri.edu; fax: (573) 882-2754; or Michael T. Henzl, Department of Biochemistry, University of Missouri–Columbia, Columbia, MO 65211, USA; e-mail: henzlm{at}missouri.edu; fax: (573) 884-4812.

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.03571004.


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 Sci.Home page
M. T. Henzl and J. J. Tanner
Solution structure of Ca2+-free rat {alpha}-parvalbumin
Protein Sci., March 1, 2008; 17(3): 431 - 438.
[Abstract] [Full Text] [PDF]

Home page
 Protein Sci.Home page
M. T. Henzl and J. J. Tanner
Solution structure of Ca2+-free rat beta-parvalbumin (oncomodulin)
Protein Sci., September 1, 2007; 16(9): 1914 - 1926.
[Abstract] [Full Text] [PDF]


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