Crystal structure of a probable LacI family transcriptional regulator from Corynebacterium glutamicum

Bonanno, J.B.; Freeman, Jeremy A.; Bain, K.T.; Mendoza, M.; Ozyurt, S.; Smith, Duncan J.; Wasserman, S.R.; Sauder, J.M.; Burley, S.K.; Almo, S.C.

doi:10.2210/pdb3bil/pdb

2007

DOI: 10.2210/pdb3bil/pdb

|View full text |Cite

Crystal structure of a probable LacI family transcriptional regulator from Corynebacterium glutamicum

J.B. Bonanno¹,

Jeremy A. Freeman²,

K.T. Bain³

et al.

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...

Citation Types

Supporting

Mentioning

Contrasting

Year Published

2013

Publication Types

Select...

Article1

Relationship

Self Cite0

Independent1

Authors

Journals

Cited by 1 publication

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

Multiple Co-Evolutionary Networks Are Supported by the Common Tertiary Scaffold of the LacI/GalR Proteins

Parente

Swint-Kruse

2013

PLoS ONE

View full text Add to dashboard Cite

Protein families might evolve paralogous functions on their common tertiary scaffold in two ways. First, the locations of functionally-important sites might be “hard-wired” into the structure, with novel functions evolved by altering the amino acid (e.g. Ala vs Ser) at these positions. Alternatively, the tertiary scaffold might be adaptable, accommodating a unique set of functionally important sites for each paralogous function. To discriminate between these possibilities, we compared the set of functionally important sites in the six largest paralogous subfamilies of the LacI/GalR transcription repressor family. LacI/GalR paralogs share a common tertiary structure, but have low sequence identity (≤30%), and regulate a variety of metabolic processes. Functionally important positions were identified by conservation and co-evolutionary sequence analyses. Results showed that conserved positions use a mixture of the “hard-wired” and “accommodating” scaffold frameworks, but that the co-evolution networks were highly dissimilar between any pair of subfamilies. Therefore, the tertiary structure can accommodate multiple networks of functionally important positions. This possibility should be included when designing and interpreting sequence analyses of other protein families. Software implementing conservation and co-evolution analyses is available at https://sourceforge.net/projects/coevolutils/.

show abstract

Multiple Co-Evolutionary Networks Are Supported by the Common Tertiary Scaffold of the LacI/GalR Proteins

Parente

Swint-Kruse

2013

PLoS ONE

View full text Add to dashboard Cite

show abstract

scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.

Contact Info

hi@scite.ai

10624 S. Eastern Ave., Ste. A-614

Henderson, NV 89052, USA

Blog Terms and Conditions API Terms Privacy Policy Contact Cookie Preferences Do Not Sell or Share My Personal Information

Made with 💙 for researchers

Part of the Research Solutions Family.

Crystal structure of a probable LacI family transcriptional regulator from Corynebacterium glutamicum

Cited by 1 publication

References 0 publications

Multiple Co-Evolutionary Networks Are Supported by the Common Tertiary Scaffold of the LacI/GalR Proteins

Multiple Co-Evolutionary Networks Are Supported by the Common Tertiary Scaffold of the LacI/GalR Proteins

Contact Info

Product

Resources

About