Open AccessStructures of the first representatives of Pfam family PF06684 (DUF1185) reveal a novel variant of the Bacillus chorismate mutase fold and suggest a role in amino‐acid metabolism
Author(s) -
Bakolitsa Constantina,
Kumar Abhinav,
Jin Kevin K.,
McMullan Daniel,
Krishna S. Sri,
Miller Mitchell D.,
Abdubek Polat,
Acosta Claire,
Astakhova Tamara,
Axelrod Herbert L.,
Burra Prasad,
Carlton Dennis,
Chen Connie,
Chiu HsiuJu,
Clayton Thomas,
Das Debanu,
Deller Marc C.,
Duan Lian,
Elias Ylva,
Ellrott Kyle,
Ernst Dustin,
Farr Carol L.,
Feuerhelm Julie,
Grant Joanna C.,
Grzechnik Anna,
Grzechnik Slawomir K.,
Han Gye Won,
Jaroszewski Lukasz,
Johnson Hope A.,
Klock Heath E.,
Knuth Mark W.,
Kozbial Piotr,
Marciano David,
Morse Andrew T.,
Murphy Kevin D.,
Nigoghossian Edward,
Nopakun Amanda,
Okach Linda,
Paulsen Jessica,
Puckett Christina,
Reyes Ron,
Rife Christopher L.,
Sefcovic Natasha,
Tien Henry J.,
Trame Christine B.,
Trout Christina V.,
Van Den Bedem Henry,
Weekes Dana,
White Aprilfawn,
Xu Qingping,
Hodgson Keith O.,
Wooley John,
Elsliger MarcAndre,
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/s1744309109050647
Subject(s) - structural genomics , context (archaeology) , random hexamer , biochemistry , isomerase , genome , chemistry , biology , protein structure , crystallography , computational biology , gene , paleontology
The crystal structures of BB2672 and SPO0826 were determined to resolutions of 1.7 and 2.1 Å by single‐wavelength anomalous dispersion and multiple‐wavelength anomalous dispersion, respectively, using the semi‐automated high‐throughput pipeline of the Joint Center for Structural Genomics (JCSG) as part of the NIGMS Protein Structure Initiative (PSI). These proteins are the first structural representatives of the PF06684 (DUF1185) Pfam family. Structural analysis revealed that both structures adopt a variant of the Bacillus chorismate mutase fold (BCM). The biological unit of both proteins is a hexamer and analysis of homologs indicates that the oligomer interface residues are highly conserved. The conformation of the critical regions for oligomerization appears to be dependent on pH or salt concentration, suggesting that this protein might be subject to environmental regulation. Structural similarities to BCM and genome‐context analysis suggest a function in amino‐acid synthesis.