4.7 Article

Metalloproteomics: High-throughput structural and functional annotation of proteins in structural genomics

Journal

STRUCTURE
Volume 13, Issue 10, Pages 1473-1486

Publisher

CELL PRESS
DOI: 10.1016/j.str.2005.07.014

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Funding

  1. NIBIB NIH HHS [P41-EB-01979] Funding Source: Medline
  2. NIGMS NIH HHS [U54-GM-74945] Funding Source: Medline

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A high-throughput method for measuring transition metal content based on quantitation of X-ray fluorescence signals was used to analyze 654 proteins selected as targets by the New York Structural GenomiX Research Consortium. Over 10% showed the presence of transition metal atoms in stoichiometric amounts; these totals as well as the abundance distribution are similar to those of the Protein Data Bank. Bioinformatics analysis of the identified metalloproteins in most cases supported the metalloprotein annotation; identification of the conserved metal binding motif was also shown to be useful in verifying structural models of the proteins. Metalloproteomics provides a rapid structural and functional annotation for these sequences and is shown to be similar to 95% accurate in predicting the presence or absence of stoichiometric metal content. The project's goal is to assay at least 1 member from each Pfam family; approximately 500 Pfam families have been characterized with respect to transition metal content so far.

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