4NC9

Crystal structure of phosphatidyl mannosyltransferase PimA

Summary for 4NC9

• Entry DOI: 10.2210/pdb4nc9/pdb
• Related: 4N9W
• Descriptor: GDP-mannose-dependent alpha-(1-2)-phosphatidylinositol mannosyltransferase (2 entities in total)
• Functional Keywords: gt-b, transferase
• Biological source: Mycobacterium smegmatis
• Cellular location: Cell membrane ; Single-pass membrane protein : A0QWG6
• Total number of polymer chains: 4
• Total formula weight: 166164.75

Authors

Giganti, D.,Albesa-Jove, D.,Bellinzoni, M.,Guerin, M.E.,Alzari, P.M. (deposition date: 2013-10-24, release date: 2014-11-12, Last modification date: 2023-09-20)

Primary citation

Giganti, D.,Albesa-Jove, D.,Urresti, S.,Rodrigo-Unzueta, A.,Martinez, M.A.,Comino, N.,Barilone, N.,Bellinzoni, M.,Chenal, A.,Guerin, M.E.,Alzari, P.M.
Secondary structure reshuffling modulates glycosyltransferase function at the membrane.
Nat.Chem.Biol., 11:16-18, 2015

PubMed Abstract: Secondary structure refolding is a key event in biology as it modulates the conformation of many proteins in the cell, generating functional or aberrant states. The crystal structures of mannosyltransferase PimA reveal an exceptional flexibility of the protein along the catalytic cycle, including β-strand-to-α-helix and α-helix-to-β-strand transitions. These structural changes modulate catalysis and are promoted by interactions of the protein with anionic phospholipids in the membrane.

PubMed: 25402770
DOI: 10.1038/nchembio.1694

Experimental method

X-RAY DIFFRACTION (3.192 Å)