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


     

Published online before print March 7, 2006, 10.1110/ps.052037006
Protein Science (2006), 15:914-920. Published by Cold Spring Harbor Laboratory Press. Copyright © 2006 The Protein Society
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental Research Data
Right arrow All Versions of this Article:
ps.052037006v1
15/4/914    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 Google Scholar
Google Scholar
Right arrow Articles by Manjasetty, B. A.
Right arrow Articles by Heinemann, U.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Manjasetty, B. A.
Right arrow Articles by Heinemann, U.
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 STRUCTURE REPORTS

Crystal structure of Homo sapiens PTD012 reveals a zinc-containing hydrolase fold

Babu A. Manjasetty1,2,7, Konrad Büssow4,5, Martin Fieber-Erdmann1,3, Yvette Roske2,4, Johan Gobom5, Christoph Scheich4,5, Frank Götz2,4, Frank H. Niesen4,6 and Udo Heinemann2,3

1 Protein Structure Factory, Berlin 12489, Germany
2 Max-Delbrück-Centrum für Molekulare Medizin, Berlin 13092, Germany
3 Institut für Chemie und Biochemie, Berlin 14195, Germany
4 Protein Structure Factory, Berlin 14059, Germany
5 Max-Planck-Institut für Molekulare Genetik, Berlin 14195, Germany
6 Institut für Medizinische Physik und Biophysik, Charité Universitätsmedizin Berlin, Berlin 10098, Germany

(RECEIVED December 13, 2005; FINAL REVISION December 13, 2005; ACCEPTED December 16, 2005)

The human protein PTD012 is the longer product of an alternatively spliced gene and was described to be localized in the nucleus. The X-ray structure analysis at 1.7 Å resolution of PTD012 through SAD phasing reveals a monomeric protein and a novel fold. The shorter splice form was also studied and appears to be unfolded and non-functional. The structure of PTD012 displays an {alpha}betabeta{alpha} four-layer topology. A metal ion residing between the central beta-sheets is partially coordinated by three histidine residues. X-ray absorption near-edge structure (XANES) analysis identifies the PTD012-bound ion as Zn2+. Tetrahedral coordination of the ion is completed by the carboxylate oxygen atom of an acetate molecule taken up from the crystallization buffer. The binding of Zn2+ to PTD012 is reminiscent of zinc-containing enzymes such as carboxypeptidase, carbonic anhydrase, and beta-lactamase. Biochemical assays failed to demonstrate any of these enzyme activities in PTD012. However, PTD012 exhibits ester hydrolase activity on the substrate p-nitrophenyl acetate.

Keywords: PTD012 family; alternative splicing; splice variant; structural genomics; Zn-binding site; ester hydrolase


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?




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2006 by The Protein Society.