HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 279, Issue 37, 39094-39104, September 10, 2004

This Article Full Text Full Text (PDF) All Versions of this Article: 279/37/39094    most recent M403863200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Lou, X. Articles by Hao, Q. Search for Related Content PubMed PubMed Citation Articles by Lou, X. Articles by Hao, Q. Social Bookmarking                      What's this?

The Atomic Resolution Crystal Structure of Atratoxin Determined by Single Wavelength Anomalous Diffraction Phasing^*

Xiaohua Lou¶||, Qun Liu||**, Xiongying Tu¶, Jing Wang¶, Maikun Teng¶, Liwen Niu¶, David J. Schuller**, Qingqiu Huang**, and Quan Hao**¶¶

From the Key Laboratory of Structural Biology, Chinese Academy of Sciences, the Department of Molecular and Cell Biology, School of Life Sciences, ^¶Hefei National Laboratory for Physical Sciences at Microscale, University of Science and Technology of China, 96 Jinzhai Road, Hefei, Anhui 230026, China, and the ^**Department of Molecular Biology and Genetics, Cornell University, Ithaca, New York 14853

By using single wavelength anomalous diffraction phasing based on the anomalous signal from copper atoms, the crystal structure of atratoxin was determined at the resolution of 1.5 Å and was refined to an ultrahigh resolution of 0.87 Å. The ultrahigh resolution electron density maps allowed the modeling of 38 amino acid residues in alternate conformations and the location of 322 of 870 possible hydrogen atoms. To get accurate information at the atomic level, atratoxin-b (an analog of atratoxin with reduced toxicity) was also refined to an atomic resolution of 0.92 Å. By the sequence and structural comparison of these two atratoxins, Arg³³ and Arg³⁶ were identified to be critical to their varied toxicity. The effect of copper ions on the distribution of hydrogen atoms in atratoxin was discussed, and the interactions between copper ions and protein residues were analyzed based on a statistical method, revealing a novel pentahedral copper-binding motif.

Received for publication, April 7, 2004 , and in revised form, June 17, 2004.

The atomic coordinates and structure factors (codes 1V6P and 1VB0) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AY471578 and AY471579.

^* This work was supported in part by the MacCHESS facility, National Center for Research Resources Grant RR-01646 from the National Institutes of Health (to Q. Hao). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^|| Both authors contributed equally to this work.

Supported by National Natural Science Foundation of China Research Grants 39870108, 30025012, 39970175, and GG0854, the 973 and 863 Plans of the Ministry of Science and Technology of China Grants G1999075603 and 2001AA233021, and the Chinese Academy of Sciences Grants STZ-2-07, STZ98-2-12, and STZ01-29.

To whom correspondence may be addressed. Tel.: 86-551-3603046; Fax: 86-551-3603046; E-mail: lwniu{at}ustc.edu.cn.

^¶¶ To whom correspondence may be addressed. Tel.: 607-254-8983; Fax: 607-255-9001; E-mail: qh22{at}cornell.edu.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?