Open AccessStructure of the first representative of Pfam family PF04016 (DUF364) reveals enolase and Rossmann‐like folds that combine to form a unique active site with a possible role in heavy‐metal chelation
Author(s) -
Miller Mitchell D.,
Aravind L.,
Bakolitsa Constantina,
Rife Christopher L.,
Carlton Dennis,
Abdubek Polat,
Astakhova Tamara,
Axelrod Herbert L.,
Chiu HsiuJu,
Clayton Thomas,
Deller Marc C.,
Duan Lian,
Feuerhelm Julie,
Grant Joanna C.,
Han Gye Won,
Jaroszewski Lukasz,
Jin Kevin K.,
Klock Heath E.,
Knuth Mark W.,
Kozbial Piotr,
Krishna S. Sri,
Kumar Abhinav,
Marciano David,
McMullan Daniel,
Morse Andrew T.,
Nigoghossian Edward,
Okach Linda,
Reyes Ron,
Van Den Bedem Henry,
Weekes Dana,
Xu Qingping,
Hodgson Keith O.,
Wooley John,
Elsliger MarcAndré,
Deacon Ashley M.,
Godzik Adam,
Lesley Scott A.,
Wilson Ian A.
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110007517
Subject(s) - context (archaeology) , active site , chemistry , structural genomics , geobacillus stearothermophilus , protein structure , stereochemistry , biochemistry , computational biology , crystallography , biology , enzyme , paleontology , thermophile
The crystal structure of Dhaf4260 from Desulfitobacterium hafniense DCB‐2 was determined by single‐wavelength anomalous diffraction (SAD) to a resolution of 2.01 Å using the semi‐automated high‐throughput pipeline of the Joint Center for Structural Genomics (JCSG) as part of the NIGMS Protein Structure Initiative (PSI). This protein structure is the first representative of the PF04016 (DUF364) Pfam family and reveals a novel combination of two well known domains (an enolase N‐terminal‐like fold followed by a Rossmann‐like domain). Structural and bioinformatic analyses reveal partial similarities to Rossmann‐like methyltransferases, with residues from the enolase‐like fold combining to form a unique active site that is likely to be involved in the condensation or hydrolysis of molecules implicated in the synthesis of flavins, pterins or other siderophores. The genome context of Dhaf4260 and homologs additionally supports a role in heavy‐metal chelation.