X-ray Crystallographic Structure of BshC, a Unique Enzyme Involved in Bacillithiol Biosynthesis

[Image: see text] Bacillithiol is produced by many Gram-positive bacteria via a pathway utilizing the enzymes BshA, BshB, and BshC. Here we report the 1.77 Å resolution crystal structure of BshC, the putative cysteine ligase in bacillithiol production. The structure reveals that BshC contains a core...

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Autores principales: VanDuinen, Andrew J., Winchell, Kelsey R., Keithly, Mary E., Cook, Paul D.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2014
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4303302/
https://www.ncbi.nlm.nih.gov/pubmed/25496067
http://dx.doi.org/10.1021/bi501394q
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author VanDuinen, Andrew J.
Winchell, Kelsey R.
Keithly, Mary E.
Cook, Paul D.
author_facet VanDuinen, Andrew J.
Winchell, Kelsey R.
Keithly, Mary E.
Cook, Paul D.
author_sort VanDuinen, Andrew J.
collection PubMed
description [Image: see text] Bacillithiol is produced by many Gram-positive bacteria via a pathway utilizing the enzymes BshA, BshB, and BshC. Here we report the 1.77 Å resolution crystal structure of BshC, the putative cysteine ligase in bacillithiol production. The structure reveals that BshC contains a core Rossmann fold with connecting peptide motifs (CP1 and CP2) and a unique α-helical coiled-coil domain that facilitates dimerization. The model contains citrate and glycerol in the canonical active site and ADP in a second binding pocket. The overall structure and bound ligands give insight into the function of this unique enzyme.
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spelling pubmed-43033022015-12-12 X-ray Crystallographic Structure of BshC, a Unique Enzyme Involved in Bacillithiol Biosynthesis VanDuinen, Andrew J. Winchell, Kelsey R. Keithly, Mary E. Cook, Paul D. Biochemistry [Image: see text] Bacillithiol is produced by many Gram-positive bacteria via a pathway utilizing the enzymes BshA, BshB, and BshC. Here we report the 1.77 Å resolution crystal structure of BshC, the putative cysteine ligase in bacillithiol production. The structure reveals that BshC contains a core Rossmann fold with connecting peptide motifs (CP1 and CP2) and a unique α-helical coiled-coil domain that facilitates dimerization. The model contains citrate and glycerol in the canonical active site and ADP in a second binding pocket. The overall structure and bound ligands give insight into the function of this unique enzyme. American Chemical Society 2014-12-12 2015-01-20 /pmc/articles/PMC4303302/ /pubmed/25496067 http://dx.doi.org/10.1021/bi501394q Text en Copyright © 2014 American Chemical Society This is an open access article published under an ACS AuthorChoice License (http://pubs.acs.org/page/policy/authorchoice_termsofuse.html) , which permits copying and redistribution of the article or any adaptations for non-commercial purposes.
spellingShingle VanDuinen, Andrew J.
Winchell, Kelsey R.
Keithly, Mary E.
Cook, Paul D.
X-ray Crystallographic Structure of BshC, a Unique Enzyme Involved in Bacillithiol Biosynthesis
title X-ray Crystallographic Structure of BshC, a Unique Enzyme Involved in Bacillithiol Biosynthesis
title_full X-ray Crystallographic Structure of BshC, a Unique Enzyme Involved in Bacillithiol Biosynthesis
title_fullStr X-ray Crystallographic Structure of BshC, a Unique Enzyme Involved in Bacillithiol Biosynthesis
title_full_unstemmed X-ray Crystallographic Structure of BshC, a Unique Enzyme Involved in Bacillithiol Biosynthesis
title_short X-ray Crystallographic Structure of BshC, a Unique Enzyme Involved in Bacillithiol Biosynthesis
title_sort x-ray crystallographic structure of bshc, a unique enzyme involved in bacillithiol biosynthesis
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4303302/
https://www.ncbi.nlm.nih.gov/pubmed/25496067
http://dx.doi.org/10.1021/bi501394q
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