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Crystal structure of Bacillus subtilis ioli shows endonuclase IV fold with altered Zn binding

Crystal structure of Bacillus subtilis ioli shows endonuclase IV fold with altered Zn binding <h1>Introduction.</h1> Myo‐Inositol is commonly found in nature, particularly in soil. Various microorganisms, including soil bacteria, are able to grow on inositol as the sole source of carbon. 1 These findings suggest that myo‐inositol catabolism might be conserved among these different microorganisms, although the molecular genetics of the many genes involved have not yet been well characterized. 1 In B. subtilis genome, the inositol catabolism pathway consists of several genes including iolI. The iolI gene (NCBI accession P42419) codes for a conserved 278‐residue protein of unknown function that shows no sequence homology with proteins of known structure [cluster 2500 in PROTOMAP, ]. Therefore, it was suggested that this protein may display a previously unobserved structural fold. There are sequence homologies to other structurally undetermined proteins, predominately from the B. subtilis family, including one in the inositol catabolism pathway ( iolH ). PSI‐BLAST 2 analysis revealed 335 sequence homologs of IolI in bacteria, archaea, and eukaryota (using inclusion threshold 0.005). As a part of the Midwest Center for Structural Genomics (MCSG) initiative (), we have determined the crystal structure of IolI protein at 1.6 Å resolution by using a semiautomated, high‐throughput approach. After acquisition of the crystallographic data, structure solution http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Proteins: Structure Function and Bioinformatics Wiley

Crystal structure of Bacillus subtilis ioli shows endonuclase IV fold with altered Zn binding

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References (12)

Publisher
Wiley
Copyright
Copyright © 2002 Wiley Subscription Services
ISSN
0887-3585
eISSN
1097-0134
DOI
10.1002/prot.10159
pmid
12112707
Publisher site
See Article on Publisher Site

Abstract

<h1>Introduction.</h1> Myo‐Inositol is commonly found in nature, particularly in soil. Various microorganisms, including soil bacteria, are able to grow on inositol as the sole source of carbon. 1 These findings suggest that myo‐inositol catabolism might be conserved among these different microorganisms, although the molecular genetics of the many genes involved have not yet been well characterized. 1 In B. subtilis genome, the inositol catabolism pathway consists of several genes including iolI. The iolI gene (NCBI accession P42419) codes for a conserved 278‐residue protein of unknown function that shows no sequence homology with proteins of known structure [cluster 2500 in PROTOMAP, ]. Therefore, it was suggested that this protein may display a previously unobserved structural fold. There are sequence homologies to other structurally undetermined proteins, predominately from the B. subtilis family, including one in the inositol catabolism pathway ( iolH ). PSI‐BLAST 2 analysis revealed 335 sequence homologs of IolI in bacteria, archaea, and eukaryota (using inclusion threshold 0.005). As a part of the Midwest Center for Structural Genomics (MCSG) initiative (), we have determined the crystal structure of IolI protein at 1.6 Å resolution by using a semiautomated, high‐throughput approach. After acquisition of the crystallographic data, structure solution

Journal

Proteins: Structure Function and Bioinformatics – Wiley

Published: Jan 1, 2002

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