Structure-function relationships in monotopic phosphoglycosyl transferases

Complex glycans play essential roles in prokaryotic and eukaryotic biology. While this ubiquitous post-translational modification takes a diversity of forms, many glycoconjugate biosynthesis pathway across domains of life follows a common logic. Glycan assembly is initiated by a phosphoglycosyl transferase (PGT) that transfers a phosphosugar from a nucleotide donor to a polyprenol phosphate (PrenP) chain embedded in the membrane. The PrenPP-sugar product is elaborated by downstream glycosyltransferases, transferred across the membrane and ultimately appended to various acceptor molecules. The PGTs initiating glycan assembly adopt diverse membrane architectures. An extensive superfamily of PGTs, elucidated in part by this thesis, is exemplified by PglC from the Gramnegative pathogen, Campylobacterjejuni. PglC comprises a globular cytosolic domain and an N-terminal membrane-resident domain.

Name thesis:degree_name

Doctoral

Department dc:contributor.department

Massachusetts Institute of Technology. Department of Biology

Grantor dc:publisher

Massachusetts Institute of Technology

Year dc:date.issued

2019

Author dc:creator

• Entova, Sonya.

Advisor dc:contributor.advisor

• Barbara Imperiali.

• Biology.

Statement dc:rights

• MIT theses are protected by copyright. They may be viewed, downloaded, or printed from this source but further reproduction or distribution in any format is prohibited without written permission.

Licence dc:rights.uri

• http://dspace.mit.edu/handle/1721.1/7582

Language dc:language.iso

eng

Handle dc:identifier.uri

https://hdl.handle.net/1721.1/122206

OAI identifier oai:identifier

oai:dspace.mit.edu:1721.1/122206