Structure of superlong, ice-binding protein reported | August 21, 2017 Issue - Vol. 95 Issue 33 | Chemical & Engineering News
Volume 95 Issue 33 | p. 6 | News of The Week
Issue Date: August 21, 2017 | Web Date: August 15, 2017

Structure of superlong, ice-binding protein reported

Adhesin protein helps Antarctic bacteria stick to ice and photosynthetic diatoms at same time
Department: Science & Technology
Keywords: structural biology, X-ray crystallography, ice, bacteria, Antarctica

After a decade of persistent effort, researchers have obtained the first complete structure of a bacterial protein with one of the longest folded conformations of any known protein—600 nm in length.

The protein is expressed on the surface of a bacterium called Marinomonas primoryensis, which lives in waters in and around Antarctica. The biomolecule, a so-called adhesin protein named M. primoryensis ice-binding protein (MpIBP), latches onto the underside of ice shelves, a near-surface location where . . .

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