Cysteine Desulfurases Mediating Sulfur Trafficking for the Biosynthesis of Fe-S Clusters

Bacteria have developed systems to safely traffic intracellular iron and sulfur for the biosynthesis of Fe-S clusters. These dedicated pathways guarantee the recruitment of individual components, their assembly into clusters and delivery to final targets. Despite variations on pathway composition, all systems identified to date include the participation of at least a cysteine desulfurase and an Fe-S cluster scaffold. The first step in sulfur mobilization for the assembly of Fe-S clusters as well as other thiocofactors within the cell involves a PLP-dependent enzymatic mechanism, catalyzed by cysteine desulfurases. There have been identified two groups of cysteine desulfurases: group I - NifS and IscS and group II - SufS and CsdA. Tertiary structural signature motifs within these groups provide a rationale for their catalytic differences and specific interactions that occurs between the cysteine desulfurases and sulfur acceptors.

Grantor dc:publisher

Wake Forest University

Year dc:date.issued

2013

Author dc:creator

• Selbach, Bruna

• Cysteine Desulfurases

Language dc:language.iso

en

Handle dc:identifier.uri

http://hdl.handle.net/10339/39132

OAI identifier oai:identifier

oai:wakespace.lib.wfu.edu:10339/39132